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1
Xavier-Filho, J., and F. A. Paiva Campos. "Genes encoding protease inhibitors." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S58—S59. http://dx.doi.org/10.1007/bf02671572.
Повний текст джерела
2
Reid, Vernita J., Louwrens W. Theron, Maret du Toit, and Benoit Divol. "Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384." Applied and Environmental Microbiology 78, no. 19 (July 20, 2012): 6838–49. http://dx.doi.org/10.1128/aem.00505-12.
Повний текст джерелаАнотація:
ABSTRACTThe extracellular acid proteases of non-Saccharomyceswine yeasts may fulfill a number of roles in winemaking, which include increasing the available nitrogen sources for the growth of fermentative microbes, affecting the aroma profile of the wine, and potentially reducing protein haze formation. These proteases, however, remain poorly characterized, especially at genetic level. In this study, two extracellular aspartic protease-encoding genes were identified and sequenced, from two yeast species of enological origin: one gene fromMetschnikowia pulcherrimaIWBT Y1123, namedMpAPr1, and the other gene fromCandida apicolaIWBT Y1384, namedCaAPr1.In silicoanalysis of these two genes revealed a number of features peculiar to aspartic protease genes, and both the MpAPr1 and CaAPr1 putative proteins showed homology to proteases of yeast genera. Heterologous expression ofMpAPr1inSaccharomyces cerevisiaeYHUM272 confirmed that it encodes an aspartic protease. MpAPr1 production, which was shown to be constitutive, and secretion were confirmed in the presence of bovine serum albumin (BSA), casein, and grape juice proteins. TheMpAPr1gene was found to be present in 12 otherM. pulcherrimastrains; however, plate assays revealed that the intensity of protease activity was strain dependent and unrelated to the gene sequence.
3
Akula, Srinivas, Zhirong Fu, Sara Wernersson, and Lars Hellman. "The Evolutionary History of the Chymase Locus -a Locus Encoding Several of the Major Hematopoietic Serine Proteases." International Journal of Molecular Sciences 22, no. 20 (October 11, 2021): 10975. http://dx.doi.org/10.3390/ijms222010975.
Повний текст джерелаАнотація:
Several hematopoietic cells of the immune system store large amounts of proteases in cytoplasmic granules. The absolute majority of these proteases belong to the large family of chymotrypsin-related serine proteases. The chymase locus is one of four loci encoding these granule-associated serine proteases in mammals. The chymase locus encodes only four genes in primates, (1) the gene for a mast-cell-specific chymotryptic enzyme, the chymase; (2) a T-cell-expressed asp-ase, granzyme B; (3) a neutrophil-expressed chymotryptic enzyme, cathepsin G; and (4) a T-cell-expressed chymotryptic enzyme named granzyme H. Interestingly, this locus has experienced a number of quite dramatic expansions during mammalian evolution. This is illustrated by the very large number of functional protease genes found in the chymase locus of mice (15 genes) and rats (18 genes). A separate expansion has also occurred in ruminants, where we find a new class of protease genes, the duodenases, which are expressed in the intestinal region. In contrast, the opossum has only two functional genes in this locus, the mast cell (MC) chymase and granzyme B. This low number of genes may be the result of an inversion, which may have hindered unequal crossing over, a mechanism which may have been a major factor in the expansion within the rodent lineage. The chymase locus can be traced back to early tetrapods as genes that cluster with the mammalian genes in phylogenetic trees can be found in frogs, alligators and turtles, but appear to have been lost in birds. We here present the collected data concerning the evolution of this rapidly evolving locus, and how these changes in gene numbers and specificities may have affected the immune functions in the various tetrapod species.
4
Lewis, Janina P., Divya Iyer, and Cecilia Anaya-Bergman. "Adaptation of Porphyromonas gingivalis to microaerophilic conditions involves increased consumption of formate and reduced utilization of lactate." Microbiology 155, no. 11 (November 1, 2009): 3758–74. http://dx.doi.org/10.1099/mic.0.027953-0.
Повний текст джерелаАнотація:
Porphyromonas gingivalis, previously classified as a strict anaerobe, can grow in the presence of low concentrations of oxygen. Microarray analysis revealed alteration in gene expression in the presence of 6 % oxygen. During the exponential growth phase, 96 genes were upregulated and 79 genes were downregulated 1.4-fold. Genes encoding proteins that play a role in oxidative stress protection were upregulated, including alkyl hydroperoxide reductase (ahpCF), superoxide dismutase (sod) and thiol peroxidase (tpx). Significant changes in gene expression of proteins that mediate oxidative metabolism, such as cytochrome d ubiquinol oxidase-encoding genes, cydA and cydB, were detected. The expression of genes encoding formate uptake transporter (PG0209) and formate tetrahydrofolate ligase (fhs) was drastically elevated, which indicates that formate metabolism plays a major role under aerobic conditions. The concomitant reduction of expression of a gene encoding the lactate transporter PG1340 suggests decreased utilization of this nutrient. The concentrations of both formate and lactate were assessed in culture supernatants and cells, and they were in agreement with the results obtained at the transcriptional level. Also, genes encoding gingipain protease secretion/maturation regulator (porR) and protease transporter (porT) had reduced expression in the presence of oxygen, which also correlated with reduced protease activities under aerobic conditions. In addition, metal transport was affected, and while iron-uptake genes such as the genes encoding the haemin uptake locus (hmu) were downregulated, expression of manganese transporter genes, such as feoB2, was elevated in the presence of oxygen. Finally, genes encoding putative regulatory proteins such as extracellular function (ECF) sigma factors as well as small proteins had elevated expression levels in the presence of oxygen. As P. gingivalis is distantly related to the well-studied model organism Escherichia coli, results from our work may provide further understanding of oxygen metabolism and protection in other related bacteria belonging to the phylum Bacteroidetes.
5
Lundwall, Åke, and Adam Clauss. "Genes encoding WFDC- and Kunitz-type protease inhibitor domains: are they related?" Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1398–402. http://dx.doi.org/10.1042/bst0391398.
Повний текст джерелаАнотація:
We have previously demonstrated that the genes of SCPs (semen coagulum proteins) and the WFDC (whey acidic protein four-disulfide core)-type protease inhibitor elafin are homologous in spite of lacking similarity between their protein products. This led to the discovery of a locus on human chromosome 20, encompassing genes of the SCPs, SEMG1 (semenogelin I) and SEMG2, and 14 genes containing the sequence motif that is characteristic of WFDC-type protease inhibitors. We have now identified additional genes at the locus that are similarly organized, but which give rise to proteins containing the motif of Kunitz-type protease inhibitors. Here, we discuss the evolution of genes encoding SCPs and describe mechanisms by which they and genes with Kunitz motifs might have evolved from genes with WFDC motifs. We can also demonstrate an expansion of the WFDC locus with 0.6 Mb in the cow. The region, which seems to be specific to ruminants, contains several genes and pseudogenes with Kunitz motifs, one of which is the much-studied BPTI (bovine pancreatic trypsin inhibitor).
6
Basta, David W., David Angeles-Albores, Melanie A. Spero, John A. Ciemniecki, and Dianne K. Newman. "Heat-shock proteases promote survival of Pseudomonas aeruginosa during growth arrest." Proceedings of the National Academy of Sciences 117, no. 8 (February 6, 2020): 4358–67. http://dx.doi.org/10.1073/pnas.1912082117.
Повний текст джерелаАнотація:
When nutrients in their environment are exhausted, bacterial cells become arrested for growth. During these periods, a primary challenge is maintaining cellular integrity with a reduced capacity for renewal or repair. Here, we show that the heat-shock protease FtsH is generally required for growth arrest survival of Pseudomonas aeruginosa, and that this requirement is independent of a role in regulating lipopolysaccharide synthesis, as has been suggested for Escherichia coli. We find that ftsH interacts with diverse genes during growth and overlaps functionally with the other heat-shock protease-encoding genes hslVU, lon, and clpXP to promote survival during growth arrest. Systematic deletion of the heat-shock protease-encoding genes reveals that the proteases function hierarchically during growth arrest, with FtsH and ClpXP having primary, nonredundant roles, and HslVU and Lon deploying a secondary response to aging stress. This hierarchy is partially conserved during growth at high temperature and alkaline pH, suggesting that heat, pH, and growth arrest effectively impose a similar type of proteostatic stress at the cellular level. In support of this inference, heat and growth arrest act synergistically to kill cells, and protein aggregation appears to occur more rapidly in protease mutants during growth arrest and correlates with the onset of cell death. Our findings suggest that protein aggregation is a major driver of aging and cell death during growth arrest, and that coordinated activity of the heat-shock response is required to ensure ongoing protein quality control in the absence of growth.
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Bidochka, Michael J., and Michael J. Melzer. "Genetic polymorphisms in three subtilisin-like protease isoforms (Pr1A, Pr1B, and Pr1C) from Metarhizium strains." Canadian Journal of Microbiology 46, no. 12 (December 1, 2000): 1138–44. http://dx.doi.org/10.1139/w00-112.
Повний текст джерелаАнотація:
Restriction fragment length polymorphisms (RFLP) were examined in three isoforms of a gene family encoding subtilisin-like proteases (Pr1A, Pr1B, and Pr1C) in several isolates of the entomopathogenic fungus Metarhizium anisopliae. RFLP variation was not observed in any of the Pr1 genes from isolates within the same genetically related group. Between genetically related groups and between isolates from disparate geographical areas, the greatest variation in RFLP patterns was observed for Pr1A. When variation does occur at Pr1B and Pr1C, it was generally observed at an EcoRI site. Metarhizium anisopliae var. majus strain 473 and a M. flavoviride isolate were most dissimilar in RFLP patterns at all Pr1 genes when compared to the M. anisopliae strains. We suggest that Pr1 genes represent a gene family of subtilisin-like proteases and that the Pr1A gene encodes for the ancestral subtilisin-like protease which has subsequently duplicated and rearranged within the genome.Key words: Metarhizium anisopliae, protease, RFLP, entomopathogen.
8
Lewis, Janina P., and Francis L. Macrina. "IS195, an Insertion Sequence-Like Element Associated with Protease Genes in Porphyromonas gingivalis." Infection and Immunity 66, no. 7 (July 1, 1998): 3035–42. http://dx.doi.org/10.1128/iai.66.7.3035-3042.1998.
Повний текст джерелаАнотація:
ABSTRACT Porphyromonas gingivalis is recognized as an important etiologic agent in adult and early-onset periodontal disease. Proteases produced by this organism contribute to its virulence in mice. Protease-encoding genes have been shown to contain multiple copies of repeated nucleotide sequences. These conserved sequences have also been found in hemagglutinin genes. In the process of studying the genetic loci containing the conserved repeated sequences, we have characterized a prtP gene homolog from P. gingivalis W83 encoding a cysteine protease with Lys-X specificity. However, thisprtP gene was interrupted by an insertion sequence-like element which we designated IS195. Furthermore, IS195 and another element, IS1126, were present downstream of prtP gene homologs (kgp) found inP. gingivalis H66 and 381. IS195, a 1,068-bp insertion sequence-like element, contained 11-bp inverted repeats at its termini and was bordered by 9-bp direct repeats presumed to be a transposition-mediated target site duplication. Its central region contained one large open reading frame encoding a predicted 300-amino-acid protein which appeared to be a transposase. We isolated two naturally occurring variants of P. gingivalis W83, one carrying IS195 within the coding region of theprtP gene and another containing an intact prtPgene. Biochemical characterization revealed a lack of trypsin-like Lys-X specific proteolytic activity in the P. gingivalisW83 variant carrying the disrupted prtP gene. Studies using a mouse model revealed a reduction of virulence resulting from insertion of IS195 into the coding region of theprtP gene. An allelic-exchange mutant defective in theprtP gene also was constructed and tested in vivo. It displayed intermediate virulence compared to that of the wild-type andprtP::IS195 mutant strains. We conclude that the Lys-X cysteine protease contributes to virulence in soft tissue infections.
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GARNIER, Gérard, Antonella CIRCOLO, Yuanyuan XU, and John E. VOLANAKIS. "Complement C1r and C1s genes are duplicated in the mouse: differential expression generates alternative isomorphs in the liver and in the male reproductive system." Biochemical Journal 371, no. 2 (April 15, 2003): 631–40. http://dx.doi.org/10.1042/bj20021555.
Повний текст джерелаАнотація:
C1r and C1s are the serine proteases that form the catalytic unit of the C1 complex, the first component of complement. In the present study, we found that the genes encoding murine C1r and C1s are duplicated. One set of these genes, referred to as c1rA and c1sA, are primarily expressed in the liver and are therefore the homologues of the human C1r and C1s genes. The other two genes, termed c1rB and c1sB, are expressed exclusively in male reproductive tissues, specifically the coagulating gland and the prostate. The predicted C1rB and C1sB proteins share 96 and 93% amino acid identity with C1rA and C1sA respectively. Most of the substitutions are clustered in the serine protease domains, suggesting differences in catalytic efficiencies and/or substrate specificities or alternatively adaptation to different physiological environments. The high homology of C1rB and C1sB with C1rA and C1sA in the non-catalytic regions indicates that they are probably capable of assembling the C1 complex. The expression of alternative genes encoding isomorphs of activating components of complement in male reproductive tissues raises the possibility of new mechanisms of complement activation in the male genital tract or of novel functions for complement proteases in reproduction.
10
Heusel, JW, EM Scarpati, NA Jenkins, DJ Gilbert, NG Copeland, SD Shapiro, and TJ Ley. "Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene." Blood 81, no. 6 (March 15, 1993): 1614–23. http://dx.doi.org/10.1182/blood.v81.6.1614.1614.
Повний текст джерелаАнотація:
Abstract We previously have characterized a cluster of genes encoding cathepsin G (CG) and two other CG-like hematopoietic serine proteases, CGL-1 and CGL-2, on human chromosome 14. In this report, we clone and characterize a novel, related murine hematopoietic serine protease gene using human CG (hCG) cDNA as the probe. This murine gene spans approximately 2.5 kb of genomic DNA, is organized into five exons and four introns, and bears a high degree of homology to hCG at both nucleic acid (73%) and deduced amino acid (66%) levels. The predicted cDNA contains an open reading frame of 783 nucleotides that encodes a nascent protein of 261 amino acids. Processing of a putative signal (pre) peptide of 18 residues and an activation (pro) dipeptide would generate a mature enzyme of approximately 27 Kd that has an estimated pI of 12.0. Conserved residues at His44, Asp88, and Ser181 form the characteristic catalytic triad of the serine protease superfamily. The gene is tightly linked to the CTLA-1 locus on murine chromosome 14, where the serine protease genes mCCP1–4 are clustered. Expression of this gene is detected only in the bone marrow and is restricted to a small population of early myeloid cells. These findings are consistent with the identification of the gene encoding murine CG.
11
Heusel, JW, EM Scarpati, NA Jenkins, DJ Gilbert, NG Copeland, SD Shapiro, and TJ Ley. "Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene." Blood 81, no. 6 (March 15, 1993): 1614–23. http://dx.doi.org/10.1182/blood.v81.6.1614.bloodjournal8161614.
Повний текст джерелаАнотація:
We previously have characterized a cluster of genes encoding cathepsin G (CG) and two other CG-like hematopoietic serine proteases, CGL-1 and CGL-2, on human chromosome 14. In this report, we clone and characterize a novel, related murine hematopoietic serine protease gene using human CG (hCG) cDNA as the probe. This murine gene spans approximately 2.5 kb of genomic DNA, is organized into five exons and four introns, and bears a high degree of homology to hCG at both nucleic acid (73%) and deduced amino acid (66%) levels. The predicted cDNA contains an open reading frame of 783 nucleotides that encodes a nascent protein of 261 amino acids. Processing of a putative signal (pre) peptide of 18 residues and an activation (pro) dipeptide would generate a mature enzyme of approximately 27 Kd that has an estimated pI of 12.0. Conserved residues at His44, Asp88, and Ser181 form the characteristic catalytic triad of the serine protease superfamily. The gene is tightly linked to the CTLA-1 locus on murine chromosome 14, where the serine protease genes mCCP1–4 are clustered. Expression of this gene is detected only in the bone marrow and is restricted to a small population of early myeloid cells. These findings are consistent with the identification of the gene encoding murine CG.
12
Renko, Miha, Tanja Zupan, David F. Plaza, Stefanie S. Schmieder, Milica Perišić Nanut, Janko Kos, Dušan Turk, Markus Künzler та Jerica Sabotič. "Cocaprins, β-trefoil Fold Inhibitors of Cysteine and Aspartic Proteases from Coprinopsis cinerea". International Journal of Molecular Sciences 23, № 9 (28 квітня 2022): 4916. http://dx.doi.org/10.3390/ijms23094916.
Повний текст джерелаАнотація:
We introduce a new family of fungal protease inhibitors with β-trefoil fold from the mushroom Coprinopsis cinerea, named cocaprins, which inhibit both cysteine and aspartic proteases. Two cocaprin-encoding genes are differentially expressed in fungal tissues. One is highly transcribed in vegetative mycelium and the other in the stipes of mature fruiting bodies. Cocaprins are small proteins (15 kDa) with acidic isoelectric points that form dimers. The three-dimensional structure of cocaprin 1 showed similarity to fungal β-trefoil lectins. Cocaprins inhibit plant C1 family cysteine proteases with Ki in the micromolar range, but do not inhibit the C13 family protease legumain, which distinguishes them from mycocypins. Cocaprins also inhibit the aspartic protease pepsin with Ki in the low micromolar range. Mutagenesis revealed that the β2-β3 loop is involved in the inhibition of cysteine proteases and that the inhibitory reactive sites for aspartic and cysteine proteases are located at different positions on the protein. Their biological function is thought to be the regulation of endogenous proteolytic activities or in defense against fungal antagonists. Cocaprins are the first characterized aspartic protease inhibitors with β-trefoil fold from fungi, and demonstrate the incredible plasticity of loop functionalization in fungal proteins with β-trefoil fold.
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Kumar, Pawan, Tabasum Akhter, Parul Bhardwaj, Rakesh Kumar, Usha Bhardwaj, and Sudeshna Mazumdar-Leighton. "Consequences of ‘no-choice, fixed time’ reciprocal host plant switches on nutrition and gut serine protease gene expression in Pieris brassicae L. (Lepidoptera: Pieridae)." PLOS ONE 16, no. 1 (January 20, 2021): e0245649. http://dx.doi.org/10.1371/journal.pone.0245649.
Повний текст джерелаАнотація:
Rapid adaptive responses were evident from reciprocal host-plant switches on performance, digestive physiology and relative gene expression of gut serine proteases in larvae of crucifer pest P. brassicae transferred from cauliflower (CF, Brassica oleracea var. botrytis, family Brassicaceae) to an alternate host, garden nasturtium, (GN, Tropaeolum majus L., family Tropaeolaceae) and vice-versa under laboratory conditions. Estimation of nutritional indices indicated that larvae of all instars tested consumed the least food and gained less weight on CF-GN diet (significant at p≤0.05) as compared to larvae feeding on CF-CF, GN-GN and GN-CF diets suggesting that the switch to GN was nutritionally less favorable for larval growth. Nevertheless, these larvae, especially fourth instars, were adroit in utilizing and digesting GN as a new host plant type. In vitro protease assays conducted to understand associated physiological responses within twelve hours indicated that levels and properties of gut proteases were significantly influenced by type of natal host-plant consumed, change in diet as well as larval age. Activities of gut trypsins and chymotrypsins in larvae feeding on CF-GN and GN-CF diets were distinct, and represented shifts toward profiles observed in larvae feeding continuously on GN-GN and CF-CF diets respectively. Results with diagnostic protease inhibitors like TLCK, STI and SBBI in these assays and gelatinolytic zymograms indicated complex and contrasting trends in gut serine protease activities in different instars from CF-GN diet versus GN-CF diet, likely due to ingestion of plant protease inhibitors present in the new diet. Cloning and sequencing of serine protease gene fragments expressed in gut tissues of fourth instar P. brassicae revealed diverse transcripts encoding putative trypsins and chymotrypsins belonging to at least ten lineages. Sequences of members of each lineage closely resembled lepidopteran serine protease orthologs including uncharacterized transcripts from Pieris rapae. Differential regulation of serine protease genes (Pbr1-Pbr5) was observed in larval guts of P. brassicae from CF-CF and GN-GN diets while expression of transcripts encoding two putative trypsins (Pbr3 and Pbr5) were significantly different in larvae from CF-GN and GN-CF diets. These results suggested that some gut serine proteases that were differentially expressed in larvae feeding on different species of host plants were also involved in rapid adaptations to dietary switches. A gene encoding nitrile-specifier protein (nsp) likely involved in detoxification of toxic products from interactions of ingested host plant glucosinolates with myrosinases was expressed to similar levels in these larvae. Taken together, these snapshots reflected contrasts in physiological and developmental plasticity of P. brassicae larvae to nutritional challenges from wide dietary switches in the short term and the prominent role of gut serine proteases in rapid dietary adaptations. This study may be useful in designing novel management strategies targeting candidate gut serine proteases of P. brassicae using RNA interference, gene editing or crops with transgenes encoding protease inhibitors from taxonomically-distant host plants.
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Staib, Peter, Christophe Zaugg, Bernard Mignon, Johann Weber, Maria Grumbt, Sylvain Pradervand, Keith Harshman, and Michel Monod. "Differential gene expression in the pathogenic dermatophyte Arthroderma benhamiae in vitro versus during infection." Microbiology 156, no. 3 (March 1, 2010): 884–95. http://dx.doi.org/10.1099/mic.0.033464-0.
Повний текст джерелаАнотація:
Although dermatophytes are the most common agents of superficial mycoses in humans and animals, the molecular basis of the pathogenicity of these fungi is largely unknown. In vitro digestion of keratin by dermatophytes is associated with the secretion of multiple proteases, which are assumed to be responsible for their particular specialization to colonize and degrade keratinized host structures during infection. To investigate the role of individual secreted proteases in dermatophytosis, a guinea pig infection model was established for the zoophilic dermatophyte Arthroderma benhamiae, which causes highly inflammatory cutaneous infections in humans and rodents. By use of a cDNA microarray covering approximately 20–25 % of the A. benhamiae genome and containing sequences of at least 23 protease genes, we revealed a distinct in vivo protease gene expression profile in the fungal cells, which was surprisingly different from the pattern elicited during in vitro growth on keratin. Instead of the major in vitro-expressed proteases, others were activated specifically during infection. These enzymes are therefore suggested to fulfil important functions that are not exclusively associated with the degradation of keratin. Most notably, the gene encoding the serine protease subtilisin 6, which is a known major allergen in the related dermatophyte Trichophyton rubrum and putatively linked to host inflammation, was found to be the most strongly upregulated gene during infection. In addition, our approach identified other candidate pathogenicity-related factors in A. benhamiae, such as genes encoding key enzymes of the glyoxylate cycle and an opsin-related protein. Our work provides what we believe to be the first broad-scale gene expression profile in human pathogenic dermatophytes during infection, and points to putative virulence-associated mechanisms that make these micro-organisms the most successful aetiological agents of superficial mycoses.
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Hensel, Michael, Christoph M. Tang, Herbert N. Arst Jr., and David W. Holden. "Regulation of fungal extracellular proteases and their role in mammalian pathogenesis." Canadian Journal of Botany 73, S1 (December 31, 1995): 1065–70. http://dx.doi.org/10.1139/b95-358.
Повний текст джерелаАнотація:
Fungal infection in the immunocompromised host is a problem of increasing importance. The virulence determinants of Aspergillus fumigatus, the major agent of invasive aspergillosis, and of Candida albicans, causing candidiasis, are not well characterized. For both pathogens, the involvement of extracellular proteases in pathogenesis is discussed. The use of gene disruption techniques to inactivate the A. fumigatus alkaline protease and metalloprotease genes has led to the firm conclusion that neither of these enzymes has a significant role in virulence. The diploid nature of C. albicans (necessitating sequential inactivation of both alleles for gene disruption studies) and the presence of a multigene family encoding secreted aspartyl proteases has hampered progress in understanding the role of proteases in virulence. We discuss the involvement of wide-domain regulators in the control of protease production and give an example of how one of these regulators (encoded by the areA gene) has been used in virulence studies. Key words: Aspergillus, Candida, proteases, gene regulation.
16
Obichi, E. A., and V. Ezebuiro. "Protease-Producing Bacteria Isolated from Beans Effluent-Impacted Soil Habour apr and npr Protease Encoding Genes." International Journal of Scientific and Research Publications 12, no. 9 (September 24, 2022): 373–79. http://dx.doi.org/10.29322/ijsrp.12.09.2022.p12949.
Повний текст джерела
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Brouta, Frédéric, Frédéric Descamps, Michel Monod, Sandy Vermout, Bertrand Losson, and Bernard Mignon. "Secreted Metalloprotease Gene Family of Microsporum canis." Infection and Immunity 70, no. 10 (October 2002): 5676–83. http://dx.doi.org/10.1128/iai.70.10.5676-5683.2002.
Повний текст джерелаАнотація:
ABSTRACT Keratinolytic proteases secreted by dermatophytes are likely to be virulence-related factors. Microsporum canis, the main agent of dermatophytosis in dogs and cats, causes a zoonosis that is frequently reported. Using Aspergillus fumigatus metalloprotease genomic sequence (MEP) as a probe, three genes (MEP1, MEP2, and MEP3) were isolated from an M. canis genomic library. They presented a quite-high percentage of identity with both A. fumigatus MEP and Aspergillus oryzae neutral protease I genes. At the amino acid level, they all contained an HEXXH consensus sequence, confirming that these M. canis genes (MEP genes) encode a zinc-containing metalloprotease gene family. Furthermore, MEP3 was found to be the gene encoding a previously isolated M. canis 43.5-kDa keratinolytic metalloprotease, and was successfully expressed as an active recombinant enzyme in Pichia pastoris. Reverse transcriptase nested PCR performed on total RNA extracted from the hair of M. canis-infected guinea pigs showed that at least MEP2 and MEP3 are produced during the infection process. This is the first report describing the isolation of a gene family encoding potential virulence-related factors in dermatophytes.
18
Kot, Barbara, Piotr Szweda, Aneta Frankowska-Maciejewska, Małgorzata Piechota, and Katarzyna Wolska. "Virulence gene profiles inStaphylococcus aureusisolated from cows with subclinical mastitis in eastern Poland." Journal of Dairy Research 83, no. 2 (April 1, 2016): 228–35. http://dx.doi.org/10.1017/s002202991600008x.
Повний текст джерелаАнотація:
Staphylococcus aureusis arguably the most important pathogen involved in bovine mastitis. The aim of this study was to determine the virulence gene profiles of 124Staph. aureusisolates from subclinical mastitis in cows in eastern Poland. The presence of 30 virulence genes encoding adhesins, proteases and superantigenic toxins was investigated by PCR. The 17 different combinations of adhesin genes were identified. Occurrence ofeno(91·1%) andfib(82·3%) genes was found to be common. The frequency of other adhesion genesfnbA, fnbB, ebpswere 14·5, 50, 25%, respectively, and forcnaandbbpwere 1·6%. TheetAandetDgenes, encoding exfoliative toxins, were present in genomes of 5·6 and 8·9% isolates, respectively. ThesplAandsspA, encoding serine protease, were detected in above 90% isolates. The most frequent enterotoxin genes weresei(21%),sem(19·4%),sen(19·4%),seg(18·5%) andseo(13·7%). Thetstgene was harboured by 2·4% isolates. The 19 combinations of the superantigenic toxin genes were obtained and found in 35·5% of isolates. Three of them (seg, sei, sem, sen, seo; sec, seg, sei, sem, sen, seoandseg, sei, sem, sen) were the most frequent and found in 16·1% of the isolates. The most common virulotype, present in 17·7% of the isolates, wasfib, eno, fnbB, splA, splE, sspA. The results indicate the variation in the presence of virulence genes inStaph. aureusisolates and considerable diversity of isolates that are able to cause mastitis in cows.
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Michel, Antje, Franziska Agerer, Christof R. Hauck, Mathias Herrmann, Joachim Ullrich, Jörg Hacker, and Knut Ohlsen. "Global Regulatory Impact of ClpP Protease of Staphylococcus aureus on Regulons Involved in Virulence, Oxidative Stress Response, Autolysis, and DNA Repair." Journal of Bacteriology 188, no. 16 (August 15, 2006): 5783–96. http://dx.doi.org/10.1128/jb.00074-06.
Повний текст джерелаАнотація:
ABSTRACT Staphylococcus aureus is an important pathogen, causing a wide range of infections including sepsis, wound infections, pneumonia, and catheter-related infections. In several pathogens ClpP proteases were identified by in vivo expression technologies to be important for virulence. Clp proteolytic complexes are responsible for adaptation to multiple stresses by degrading accumulated and misfolded proteins. In this report clpP, encoding the proteolytic subunit of the ATP-dependent Clp protease, was deleted, and gene expression of ΔclpP was determined by global transcriptional analysis using DNA-microarray technology. The transcriptional profile reveals a strong regulatory impact of ClpP on the expression of genes encoding proteins that are involved in the pathogenicity of S. aureus and adaptation of the pathogen to several stresses. Expression of the agr system and agr-dependent extracellular virulence factors was diminished. Moreover, the loss of clpP leads to a complete transcriptional derepression of genes of the CtsR- and HrcA-controlled heat shock regulon and a partial derepression of genes involved in oxidative stress response, metal homeostasis, and SOS DNA repair controlled by PerR, Fur, MntR, and LexA. The levels of transcription of genes encoding proteins involved in adaptation to anaerobic conditions potentially regulated by an Fnr-like regulator were decreased. Furthermore, the expression of genes whose products are involved in autolysis was deregulated, leading to enhanced autolysis in the mutant. Our results indicate a strong impact of ClpP proteolytic activity on virulence, stress response, and physiology in S. aureus.
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Ohler, Anke, and Christoph Becker-Pauly. "TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections." Biological Chemistry 393, no. 9 (September 1, 2012): 907–14. http://dx.doi.org/10.1515/hsz-2012-0155.
Повний текст джерелаАнотація:
Abstract Proteolytic enzymes are involved in almost all biological processes reflecting their importance in health and disease. The human genome contains nearly 600 protease-encoding genes forming more than 2% of the total human proteome. The serine proteases, with about 180 members, built the oldest and second largest family of human proteases. Ten years ago, a novel serine protease family named the type II transmembrane family (TTSP) was identified. This minireview summarizes the up-to-date knowledge about the still growing TTSPs, particularly focusing on the pathophysiological functions of the family member type II transmembrane serine protease (TMPRSS) 4. Recent studies provided important data on TMPRSS4 activity associated with the spreading of influenza viruses, mediated by the cleavage of hemagglutinin. Progression and metastatic potential of several cancers is concordant with an increased expression of TMPRSS4, though being a possible diagnostic marker. However, to benefit from TMPRSS4 as a therapeutic target, more data concerning its physiological relevance are needed, as done by a specific morpholino knockdown in zebrafish embryos.
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Shai, Shaw Yung, Cheryl Woodley-Miller, Julie Chao, and Lee Chao. "Characterization of genes encoding rat tonin and a kallikrein-like serine protease." Biochemistry 28, no. 13 (June 27, 1989): 5334–43. http://dx.doi.org/10.1021/bi00439a005.
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El-Sayed, Najib M. A., and John E. Donelson. "African Trypanosomes Have Differentially Expressed Genes Encoding Homologues of theLeishmaniaGP63 Surface Protease." Journal of Biological Chemistry 272, no. 42 (October 17, 1997): 26742–48. http://dx.doi.org/10.1074/jbc.272.42.26742.
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Piotrowski, Andrew, Ping Luo, and Donald A. Morrison. "Competence for Genetic Transformation in Streptococcus pneumoniae: Termination of Activity of the Alternative Sigma Factor ComX Is Independent of Proteolysis of ComX and ComW." Journal of Bacteriology 191, no. 10 (March 13, 2009): 3359–66. http://dx.doi.org/10.1128/jb.01750-08.
Повний текст джерелаАнотація:
ABSTRACT Competence for genetic transformation in Streptococcus pneumoniae is a transient physiological state whose development is coordinated by a peptide pheromone (CSP) and its receptor, which activates transcription of two downstream genes, comX and comW, and 15 other “early” genes. ComX, a transient alternative sigma factor, drives transcription of “late” genes, many of which are essential for transformation. In vivo, ComW both stabilizes ComX against proteolysis by the ClpE-ClpP protease and stimulates its activity. Interestingly, stabilization of ComX by deletion of the gene encoding the ClpP protease did not extend the period of competence. We considered the hypothesis that the rapid decay of competence arises from a rapid loss of ComW and thus of its ComX stimulating activity, so that ComX might persist but lose its transcriptional activity. Western analysis revealed that ComW is indeed a transient protein, which is also stabilized by deletion of the gene encoding the ClpP protease. However, stabilizing both ComX and ComW did not prolong either ComX activity or the period of transformation, indicating that termination of the transcriptional activity of ComX is not dependent on proteolysis of ComW.
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Tegmark, Karin, Eva Morfeldt, and Staffan Arvidson. "Regulation of agr-Dependent Virulence Genes in Staphylococcus aureus by RNAIII from Coagulase-Negative Staphylococci." Journal of Bacteriology 180, no. 12 (June 15, 1998): 3181–86. http://dx.doi.org/10.1128/jb.180.12.3181-3186.1998.
Повний текст джерелаАнотація:
ABSTRACT Many of the genes coding for extracellular toxins, enzymes, and cell surface proteins in Staphylococcus aureus are regulated by a 510-nucleotide (nt) RNA molecule, RNAIII. Transcription of genes encoding secreted toxins and enzymes, includinghla (alpha-toxin), saeB (enterotoxin B),tst (toxic shock syndrome toxin 1), and ssp(serine protease), is stimulated, while transcription of genes encoding cell surface proteins, like spa (protein A) andfnb (fibronectin binding proteins), is repressed. Besides being a regulator, RNAIII is also an mRNA coding for staphylococcal delta-lysin. We have identified RNAIII homologs in three different coagulase-negative staphylococci (CoNS), i.e., Staphylococcus epidermidis, Staphylococcus simulans, andStaphylococcus warneri. RNAIII from these CoNS turned out to be very similar to that of S. aureus and contained open reading frames encoding delta-lysin homologs. Though a number of big insertions and/or deletions have occurred, mainly in the 5′ half of the molecules, the sequences show a high degree of identity, especially in the first 50 and last 150 nt. The CoNS RNAIII had the ability to completely repress transcription of protein A in an RNAIII-deficientS. aureus mutant and the ability to stimulate transcription of the alpha-toxin and serine protease genes. However, the stimulatory effect was impaired compared to that of S. aureus RNAIII, suggesting that these regulatory functions are independent. By creating S. epidermidis-S. aureus RNAIII hybrids, we could also show that both the 5′ and 3′ halves of the RNAIII molecule are involved in the transcriptional regulation of alpha-toxin and serine protease mRNAs in S. aureus.
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Turroni, Francesca, Elena Foroni, Mary O'Connell Motherway, Francesca Bottacini, Vanessa Giubellini, Aldert Zomer, Alberto Ferrarini, et al. "Characterization of the Serpin-Encoding Gene of Bifidobacterium breve 210B." Applied and Environmental Microbiology 76, no. 10 (March 26, 2010): 3206–19. http://dx.doi.org/10.1128/aem.02938-09.
Повний текст джерелаАнотація:
ABSTRACT Members of the serpin (serine protease inhibitor) superfamily have been identified in higher multicellular eukaryotes, as well as in bacteria, although examination of available genome sequences has indicated that homologs of the bacterial serpin-encoding gene (ser) are not widely distributed. In members of the genus Bifidobacterium this gene appears to be present in at least 5, and perhaps up to 9, of the 30 species tested. Moreover, phylogenetic analysis using available bacterial and eukaryotic serpin sequences revealed that bifidobacteria produce serpins that form a separate clade. We characterized the ser 210B locus of Bifidobacterium breve 210B, which encompasses a number of genes whose deduced protein products display significant similarity to proteins encoded by corresponding loci found in several other bifidobacteria. Northern hybridization, primer extension, microarray, reverse transcription-PCR (RT-PCR), and quantitative real-time PCR (qRT-PCR) analyses revealed that a 3.5-kb polycistronic mRNA encompassing the ser 210B operon with a single transcriptional start site is strongly induced following treatment of B. breve 210B cultures with some proteases. Interestingly, transcription of other bifidobacterial ser homologs appears to be triggered by different proteases.
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Østerås, Magne, Agathe Stotz, Stefanie Schmid Nuoffer, and Urs Jenal. "Identification and Transcriptional Control of the Genes Encoding the Caulobacter crescentus ClpXP Protease." Journal of Bacteriology 181, no. 10 (May 15, 1999): 3039–50. http://dx.doi.org/10.1128/jb.181.10.3039-3050.1999.
Повний текст джерелаАнотація:
ABSTRACT The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of theC. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram-negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP). The C. crescentus clpX gene was shown by complementation analysis to be functional in Escherichia coli. However, clpX fromE. coli was not able to substitute for the essential nature of the clpX gene in C. crescentus. TheclpP and clpX genes are separated on theC. crescentus chromosome by an open reading frame pointing in the opposite direction from the clp genes, and transcription of clpP and clpX was found to be uncoupled. clpP is transcribed as a monocistronic unit with a promoter (PP1) located immediately upstream of the 5′ end of the gene and a terminator structure following its 3′ end. PP1 is under heat shock control and is induced upon entry of the cells into the stationary phase. At least three promoters forclpX (PX1, PX2, and PX3) were mapped in the clpP-clpX intergenic region. In contrast to PP1, the clpX promoters were found to be downregulated after heat shock but were also subject to growth phase control. In addition, the clpP andclpX promoters showed different activity patterns during the cell cycle. Together, these results demonstrate that the genes coding for the peptidase and the regulatory subunits of the ClpXP protease are under independent transcriptional control in C. crescentus. Determination of the numbers of ClpP and ClpX molecules per cell suggested that ClpX is the limiting component compared with ClpP.
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Liu, Yanbo, Junying Fu, Linlin Wang, Zhijun Zhao, Huihui Wang, Suna Han, Xiyu Sun, and Chunmei Pan. "Isolation, identification, and whole-genome sequencing of high-yield protease bacteria from Daqu of ZhangGong Laojiu." PLOS ONE 17, no. 4 (April 26, 2022): e0264677. http://dx.doi.org/10.1371/journal.pone.0264677.
Повний текст джерелаАнотація:
A total of 296 strains of protease-producing bacteria were isolated and purified from medium-temperature Daqu produced by ZhangGong LaoJiu Wine Co. Ltd. After calculating the ratio of transparent ring diameter to colony diameter and measuring the protease activities, a strain of high-yield protease bacteria, called DW-7, was screened out with a protease activity of 99.54 U/mL. Through morphological observation, 16S rDNA sequence analysis, and physiological and biochemical tests, the isolated bacteria DW-7 was determined to be Bacillus velezensis. In addition, whole-genome sequencing (WGS), using PacBio and the Illumina platform, was performed. Gene annotation was then conducted using the Clusters of Orthologous Groups (COG), Kyoto Encyclopedia of Genes and Genomes (KEGG), Non-Redundant Protein Sequence Database (NR), and Gene Ontology (GO) databases. The results showed that the genome of DW-7 was 3,942,829 bp long with a GC content of 46.45%. A total of 3,662 protein-encoding genes were predicted, with a total length of 3,402,822 bp. Additionally, 2,283; 2,796; and 2,127 genes were annotated in the COG, KEGG, and GO databases, respectively. A total of 196 high-yield protease genes were mainly enriched in the metabolism of alanine, aspartic acid, glutamate, glycine, serine, and threonine, as well as ABC transporter and transporter pathways.
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Liu, Yanbo, Junying Fu, Linlin Wang, Zhijun Zhao, Huihui Wang, Suna Han, Xiyu Sun, and Chunmei Pan. "Isolation, identification, and whole-genome sequencing of high-yield protease bacteria from Daqu of ZhangGong Laojiu." PLOS ONE 17, no. 4 (April 26, 2022): e0264677. http://dx.doi.org/10.1371/journal.pone.0264677.
Повний текст джерелаАнотація:
A total of 296 strains of protease-producing bacteria were isolated and purified from medium-temperature Daqu produced by ZhangGong LaoJiu Wine Co. Ltd. After calculating the ratio of transparent ring diameter to colony diameter and measuring the protease activities, a strain of high-yield protease bacteria, called DW-7, was screened out with a protease activity of 99.54 U/mL. Through morphological observation, 16S rDNA sequence analysis, and physiological and biochemical tests, the isolated bacteria DW-7 was determined to be Bacillus velezensis. In addition, whole-genome sequencing (WGS), using PacBio and the Illumina platform, was performed. Gene annotation was then conducted using the Clusters of Orthologous Groups (COG), Kyoto Encyclopedia of Genes and Genomes (KEGG), Non-Redundant Protein Sequence Database (NR), and Gene Ontology (GO) databases. The results showed that the genome of DW-7 was 3,942,829 bp long with a GC content of 46.45%. A total of 3,662 protein-encoding genes were predicted, with a total length of 3,402,822 bp. Additionally, 2,283; 2,796; and 2,127 genes were annotated in the COG, KEGG, and GO databases, respectively. A total of 196 high-yield protease genes were mainly enriched in the metabolism of alanine, aspartic acid, glutamate, glycine, serine, and threonine, as well as ABC transporter and transporter pathways.
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Hu, Yongmei, Nan Peng, Wenyuan Han, Yuxia Mei, Zhengjun Chen, Xu Feng, Yun Xiang Liang, and Qunxin She. "An archaeal protein evolutionarily conserved in prokaryotes is a zinc-dependent metalloprotease." Bioscience Reports 32, no. 6 (October 15, 2012): 609–18. http://dx.doi.org/10.1042/bsr20120074.
Повний текст джерелаАнотація:
A putative protease gene (tldD) was previously identified from studying tolerance of letD encoding the CcdB toxin of a toxin–antidote system of the F plasmid in Escherichia coli. While this gene is evolutionarily conserved in archaea and bacteria, the proteolytic activity of encoded proteins remained to be demonstrated experimentally. Here we studied Sso0660, an archaeal TldD homologue encoded in Sulfolobus solfataricus by overexpression of the recombinant protein and characterization of the purified enzyme. We found that the enzyme is active in degrading azocasein and FITC–BSA substrates. Protease inhibitor studies showed that EDTA and o-phenanthroline, two well-known metalloprotease inhibitors, either abolished completely or strongly inhibited the enzyme activity, and flame spectrometric analysis showed that a zinc ion is a cofactor of the protease. Furthermore, the protein forms disulfide bond via the Cys416 residue, yielding protein dimer that is the active form of the enzyme. These results establish for the first time that tidD genes encode zinc-containing proteases, classifying them as a family in the metalloprotease class.
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Nenno, M., K. Schumann, and W. Nagl. "Detection of rRNA and phaseolin genes on polytene chromosomes of Phaseolus coccineus by fluorescence in situ hybridization after pepsin pretreatment." Genome 37, no. 6 (December 1, 1994): 1018–21. http://dx.doi.org/10.1139/g94-144.
Повний текст джерелаАнотація:
This is the first report of fluorescence in situ hybridization (FISH) on plant polytene chromosomes. Different protease pretreatments have been tested to improve fluorescence in situ hybridization FISH on polytene chromosomes of a plant, Phaseolus coccineus, with the aim to enable the detection of low-copy genes. The structural preservation of the chromosomes and the distinctness of the FISH signals were comparatively analysed with a probe for the ribosomal RNA genes after digestion with pepsin and trypsin. The pepsin pretreatment resulted in a general loosening of chromatin with good conservation of chromosome morphology and an increased number and density of signal points. The six nucleolus organizers exhibited significant differences in condensation. The pretreatment with pepsin enabled the detection of the low-copy genes encoding the seed storage protein phaseolin.Key words: plant, Leguminosae, ribosomal RNA genes, seed storage protein genes, protease.
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Hirano, Setsu, Jun-ya Kato, Yasuo Ohnishi, and Sueharu Horinouchi. "Control of the Streptomyces Subtilisin Inhibitor Gene by AdpA in the A-Factor Regulatory Cascade in Streptomyces griseus." Journal of Bacteriology 188, no. 17 (September 1, 2006): 6207–16. http://dx.doi.org/10.1128/jb.00662-06.
Повний текст джерелаАнотація:
ABSTRACT AdpA in the A-factor regulatory cascade in Streptomyces griseus activates a number of genes required for secondary metabolism and morphological differentiation, forming an AdpA regulon. The Streptomyces subtilisin inhibitor (SSI) gene, sgiA, in S. griseus was transcribed in response to AdpA, showing that sgiA is a member of the AdpA regulon. AdpA bound a single site upstream of the sgiA promoter at approximately position −70 with respect to its transcriptional start point. Mutational analysis of the AdpA-binding site showed that the AdpA-binding site was essential for transcriptional activation. Mutants in which sgiA was disrupted had higher trypsin, chymotrypsin, metalloendopeptidase, and total protease activities than the wild-type strain, which showed that SgiA modulated the activities of these extracellularly produced proteases. Because a number of genes encoding chymotrypsins, trypsins, and metalloendopeptidases, most of which are SSI-sensitive proteases, are also under the control of AdpA, the A-factor regulatory cascade was thought to play a crucial role in modulating the extracellular protease activities by triggering simultaneous production of the proteases and their inhibitor at a specific timing during growth. Mutants in which sgiA was disrupted grew normally and formed aerial hyphae and spores with the same time course as the wild-type strain. However, exogenous addition of purified SgiA to substrate mycelium grown on agar medium resulted in a delay in aerial mycelium formation, indicating that SgiA is involved in aerial hypha formation in conjunction with proteases.
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BOUCHUT, A., C. COUSTAU, B. GOURBAL, and G. MITTA. "Compatibility in the Biomphalaria glabrata/Echinostoma caproni model: new candidate genes evidenced by a suppressive subtractive hybridization approach." Parasitology 134, no. 4 (November 13, 2006): 575–88. http://dx.doi.org/10.1017/s0031182006001673.
Повний текст джерелаАнотація:
In order to elucidate mechanisms underlying snail/echinostome compatibility, numerous molecular studies comparing transcripts and proteins of Biomphalaria glabrata susceptible or resistant to Echinostoma caproni were undertaken. These studies focused on plasma and haemocytes of the two strains and revealed that some transcripts and/or proteins were differentially expressed between strains. The aim of the present study was to develop a complementary transcriptomic approach by constructing subtractive libraries. This work revealed some candidate transcripts already identified in previous studies (calcium-binding proteins and glycolytic enzymes) as well as novel candidate transcripts that were differentially represented between strains of B. glabrata. Among these newly identified genes, we revealed several genes potentially involved in immune processes encoding proteases, protease inhibitors, a lectin, an aplysianin-like molecule, and cell adhesion molecules.
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Gosset, Guillermo, Zhongge Zhang, Samir Nayyar, William A. Cuevas, and Milton H. Saier. "Transcriptome Analysis of Crp-Dependent Catabolite Control of Gene Expression in Escherichia coli." Journal of Bacteriology 186, no. 11 (June 1, 2004): 3516–24. http://dx.doi.org/10.1128/jb.186.11.3516-3524.2004.
Повний текст джерелаАнотація:
ABSTRACT We report here the transcriptome analyses of highly expressed genes that are subject to catabolite repression or activation mediated by the cyclic AMP receptor protein (Crp). The results reveal that many operons encoding enzymes of central carbon metabolic pathways (e.g., Krebs cycle enzymes), as well as transporters and enzymes that initiate carbon metabolism, are subject to direct Crp-mediated catabolite repression. By contrast, few enzyme-encoding genes (direct regulation) but many ribosomal protein- and tRNA-encoding genes (indirect regulation) are subject to Crp-dependent glucose activation. Additionally, Crp mediates strong indirect catabolite repression of many cytoplasmic stress response proteins, including the major chaperone proteins, five ATP-dependent protease complexes, and several cold and heat shock proteins. These results were confirmed by (i) phenotypic analyses, (ii) real-time PCR studies, (iii) reporter gene fusion assays, and (iv) previously published reports about representative genes. The results serve to define and extend our appreciation of the Crp regulon.
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COPLEY, S. Kathrin, M. Sheri ALM, A. David SCHOOLEY, and E. William COURCHESNE. "Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway." Biochemical Journal 330, no. 3 (March 15, 1998): 1333–40. http://dx.doi.org/10.1042/bj3301333.
Повний текст джерелаАнотація:
A system is described for the heterologous expression of peptides in Saccharomyces cerevisiae. A synthetic gene encoding a precursor of the 41 amino acid Manduca sexta diuretic hormone (Mas-DH) was expressed at 0.8 mg/l purified peptide. A precursor of a mutant peptide of Mas-DH, Mas-DH[K22Q] was also expressed. The peptides were purified, then treated with peptidylglycine α-amidating enzyme to generate the α-amidated, mature, form of Mas-DH or Mas-DH[K22Q], which were biologically active. Successful expression of full-length Mas-DH+Gly depended upon the use of a protease-deficient yeast strain. In wild-type strains, Mas-DH+Gly was recovered only as proteolytic fragments, even in the presence of various protease inhibitors. Expression of Mas-DH+Gly in strains deficient in either the Mkc7 or the Yap3 protease reduced proteolysis, while no proteolysis of Mas-DH+Gly was detectable in a strain lacking both proteases. This protease-deficient strain may prove of general utility for expression of peptides. Analysis of recovered proteolytic fragments revealed a complex pattern of cleavage sites. Both the Yap3 and Mkc7 proteases preferred to cleave at a single Glu-Lys↓-Glu-Arg site. Analysis of secondary cleavage sites showed that Yap3 preferred to cleave after either Lys or Arg and Mkc7 after Lys. This paper is the first report on the in vivo activity and specificity of Yap3 and Mkc7 expressed at physiological levels.
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Gronover, Christian Schulze, Daniela Kasulke, Paul Tudzynski, and Bettina Tudzynski. "The Role of G Protein Alpha Subunits in the Infection Process of the Gray Mold Fungus Botrytis cinerea." Molecular Plant-Microbe Interactions® 14, no. 11 (November 2001): 1293–302. http://dx.doi.org/10.1094/mpmi.2001.14.11.1293.
Повний текст джерелаАнотація:
To identify signal transduction pathways of the gray mold fungus Botrytis cinerea involved in host infection, we used heterologous hybridization and a polymerase chain reaction (PCR)-based approach to isolate two genes (bcg1 and bcg2) encoding α subunits of heterotrimeric GTP-binding proteins. Both genes have homologues in other fungi: bcg1 is a member of the Gαi class, whereas bcg2 has similarities to the magC gene of Magnaporthe grisea and the gna-2 gene of Neurospora crassa. Reverse-transcription (RT)-PCR experiments showed clearly that both genes are expressed at very early stages in infected bean leaves. Gene replacement experiments were performed for both genes. bcg1 null mutants differ in colony morphology from the wild-type strain, do not secrete extracellular proteases, and show clearly reduced pathogenicity on bean and tomato. Conidia germination and penetration of plant tissue is not disturbed in bcg1 mutants, but the infection process stops after formation of primary lesions. In contrast, bcg2 mutants show wild-type colony morphology in axenic culture and are only slightly reduced in pathogenicity. Complementation of bcg1 mutants with the wild-type gene copy led to the full recovery of colony morphology, protease secretion, and pathogenicity on both host plants. Application of exogenous cyclic AMP restored the wild-type growth pattern of bcg1 mutants, but not the protease secretion, implicating an essential role of BCG1 in different signaling pathways.
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Powles, Joshua, Paul Savage, Edwin Wu, Katherine Karakasis, and Kenton Ko. "Motif-based evidence that a plastid translocon component acts like a rhomboid protease substrate in yeast mitochondria." Botany 89, no. 7 (July 2011): 499–511. http://dx.doi.org/10.1139/b11-039.
Повний текст джерелаАнотація:
Of the organisms with sequenced genomes, plants appear to possess the most rhomboid protease-encoding genes. However, our knowledge of processes in plants that involve rhomboid proteases and regulated intramembrane proteolysis (RIP) remains low. As expressed recently by other researchers, finding and establishing a natural substrate for a rhomboid protease represents the biggest experimental challenge. Using yeast mitochondria-based assays, a potential link between the plastid translocon component Tic40 and organellar rhomboid proteases was recently uncovered. In this particular link, rhomboid proteases appear capable of influencing the pattern of imported Tic40 in yeast mitochondria. Here, we obtained motif-oriented evidence that Tic40 acts like a rhomboid protease substrate in yeast mitochondria. A comparative analysis of sequences revealed that Tic40 may also possess similar transmembrane domain motifs found in the model substrate, Spitz. Rhomboid proteases often require these motifs to cleave substrates within intramembrane environments. Using site-directed mutagenesis and yeast mitochondria assays, the impact of mutations occurring in the motifs ASISS, GV, QP, and GVGVG of Tic40 was assessed. In terms of cleavage and changing the pattern of imported Tic40, some of the mutations showed decreased activity and a few showed enhancement. More importantly, the overall observed pattern associated with select Tic40 mutations resembled the characteristics reported for the model substrates. In particular, mutations in the Tic40 GV motif produced similar results as those observed with the Spitz GA motif, by drastically decreasing or increasing cleavage as a function of the amino acid sequence.
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NA, Byoung-Kuk, Bhaskar R. SHENAI, Puran S. SIJWALI, Youngchool CHOE, Kailash C. PANDEY, Ajay SINGH, Charles S. CRAIK, and Philip J. ROSENTHAL. "Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax." Biochemical Journal 378, no. 2 (March 1, 2004): 529–38. http://dx.doi.org/10.1042/bj20031487.
Повний текст джерелаАнотація:
Cysteine proteases play important roles in the life cycles of malaria parasites. Cysteine protease inhibitors block haemoglobin hydrolysis and development in Plasmodium falciparum, suggesting that the cysteine proteases of this major human pathogen, termed falcipains, are appropriate therapeutic targets. To expand our understanding of plasmodial proteases to Plasmodium vivax, the other prevalent human malaria parasite, we identified and cloned genes encoding the P. vivax cysteine proteases, vivapain-2 and vivapain-3, and functionally expressed the proteases in Escherichia coli. The vivapain-2 and vivapain-3 genes predicted papain-family cysteine proteases, which shared a number of unusual features with falcipain-2 and falcipain-3, including large prodomains and short N-terminal extensions on the catalytic domain. Recombinant vivapain-2 and vivapain-3 shared properties with the falcipains, including acidic pH optima, requirements for reducing conditions for activity and hydrolysis of substrates with positively charged residues at P1 and Leu at P2. Both enzymes hydrolysed native haemoglobin at acidic pH and the erythrocyte cytoskeletal protein 4.1 at neutral pH, suggesting similar biological roles to the falcipains. Considering inhibitor profiles, the vivapains were inhibited by fluoromethylketone and vinyl sulphone inhibitors that also inhibited falcipains and have demonstrated potent antimalarial activity.
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de Vries, Ronald P., Kim Burgers, Peter J. I. van de Vondervoort, Jens C. Frisvad, Robert A. Samson, and Jaap Visser. "A New Black Aspergillus Species, A. vadensis, Is a Promising Host for Homologous and Heterologous Protein Production." Applied and Environmental Microbiology 70, no. 7 (July 2004): 3954–59. http://dx.doi.org/10.1128/aem.70.7.3954-3959.2004.
Повний текст джерелаАнотація:
ABSTRACT A new species of the group of black aspergilli, Aspergillus vadensis, was analyzed for its potential as a host for homologous and heterologous protein production. Unlike the other black aspergilli, this strain does not acidify the culture medium when nitrate is the nitrogen source and only produces very low levels of extracellular proteases, mainly serine metalloproteases. The stability of A. tubingensis feruloyl esterase A (FaeA) was compared upon production in wild-type A. vadensis, A. tubingensis, and an A. niger strain in which the three main protease-encoding genes were disrupted. The production of FaeA in A. vadensis resulted in larger amounts of intact protein than production in A. tubingensis and was similar to production in an A. niger protease disruptant, confirming in vivo the low proteolytic activity of A. vadensis. The protoplast formation and transformation efficiencies of A. vadensis were much higher than those of A. niger. These characteristics make A. vadensis a very promising candidate for homologous, and possibly heterologous, protein production.
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Herbert, Silvia, Peter Barry, and Richard P. Novick. "Subinhibitory Clindamycin Differentially Inhibits Transcription of Exoprotein Genes in Staphylococcus aureus." Infection and Immunity 69, no. 5 (May 1, 2001): 2996–3003. http://dx.doi.org/10.1128/iai.69.5.2996-3003.2001.
Повний текст джерелаАнотація:
ABSTRACT It has long been known that certain antibiotics, at subinhibitory concentrations, differentially inhibit the synthesis of α-hemolysin and other staphylococcal virulence factors. In this report, we show that subinhibitory clindamycin (SBCL) eliminates production of nearly all exoproteins by Staphylococcus aureus but has virtually no effect on cytoplasmic proteins. The effect was abolished by a gene conferring resistance to macrolides-lincosamides-streptogramin B, showing that differential inhibition of protein synthesis is responsible; remarkably, however, subinhibitory clindamycin blocked production of several of the individual exoprotein genes, including spa(encoding protein A), hla (encoding α-hemolysin), andspr (encoding serine protease), at the level of transcription, suggesting that the primary effect must be differential inhibition of the synthesis of one or more regulatory proteins. In contrast to earlier reports, however, we found that subinhibitory clindamycin stimulates synthesis of coagulase and fibronectin binding protein B, also at the level of transcription.agr and sar expression was minimally affected by subinhibitory clindamycin. These effects varied from strain to strain and do not seem to be responsible for the effects of subinhibitory clindamycin on the overall exoprotein pattern.
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Larriba, Eduardo, José Martín-Nieto, and Luis Vicente Lopez-Llorca. "Gene cloning, molecular modeling, and phylogenetics of serine protease P32 and serine carboxypeptidase SCP1 from nematophagous fungiPochonia rubescensandPochonia chlamydosporia." Canadian Journal of Microbiology 58, no. 7 (July 2012): 815–27. http://dx.doi.org/10.1139/w2012-054.
Повний текст джерелаАнотація:
The fungi Pochonia chlamydosporia and Pochonia rubescens are parasites of nematode eggs and thus are biocontrol agents of nematodes. Proteolytic enzymes such as the S8 proteases VCP1 and P32, secreted during the pathogenesis of nematode eggs, are major virulence factors in these fungi. Recently, expression of these enzymes and of SCP1, a new putative S10 carboxypeptidase, was detected during endophytic colonization of barley roots by these fungi. In our study, we cloned the genomic and mRNA sequences encoding P32 from P. rubescens and SCP1 from P. chlamydosporia. P32 showed a high homology with the serine proteases Pr1A from the entomopathogenic fungus Metarhizium anisopliae and VCP1 from P. chlamydosporia (86% and 76% identity, respectively). However, the catalytic pocket of P32 showed differences in the amino acids of the substrate-recognition sites compared with the catalytic pockets of Pr1A and VCP1 proteases. Phylogenetic analysis of P32 suggests a common ancestor with protease Pr1A. SCP1 displays the characteristic features of a member of the S10 family of serine proteases. Phylogenetic comparisons show that SCP1 and other carboxypeptidases from filamentous fungi have an origin different from that of yeast vacuolar serine carboxypeptidases. Understanding protease genes from nematophagous fungi is crucial for enhancing the biocontrol potential of these organisms.
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Poulsen, Knud, Jesper Reinholdt, Christina Jespersgaard, Kit Boye, Thomas A. Brown, Majbritt Hauge, and Mogens Kilian. "A Comprehensive Genetic Study of Streptococcal Immunoglobulin A1 Proteases: Evidence for Recombination within and between Species." Infection and Immunity 66, no. 1 (January 1, 1998): 181–90. http://dx.doi.org/10.1128/iai.66.1.181-190.1998.
Повний текст джерелаАнотація:
ABSTRACT An analysis of 13 immunoglobulin A1 (IgA1) protease genes (iga) of strains of Streptococcus pneumoniae,Streptococcus oralis, Streptococcus mitis, andStreptococcus sanguis was carried out to obtain information on the structure, polymorphism, and phylogeny of this specific protease, which enables bacteria to evade functions of the predominant Ig isotype on mucosal surfaces. The analysis included cloning and sequencing of iga genes from S. oralisand S. mitis biovar 1, sequencing of an additional seveniga genes from S. sanguis biovars 1 through 4, and restriction fragment length polymorphism (RFLP) analyses of iga genes of another 10 strains of S. mitisbiovar 1 and 6 strains of S. oralis. All 13 genes sequenced had the potential of encoding proteins with molecular masses of approximately 200 kDa containing the sequence motif HEMTH and an E residue 20 amino acids downstream, which are characteristic of Zn metalloproteinases. In addition, all had a typical gram-positive cell wall anchor motif, LPNTG, which, in contrast to such motifs in other known streptococcal and staphylococcal proteins, was located in their N-terminal parts. Repeat structures showing variation in number and sequence were present in all strains and may be of relevance to the immunogenicities of the enzymes. Protease activities in cultures of the streptococcal strains were associated with species of different molecular masses ranging from 130 to 200 kDa, suggesting posttranslational processing possibly as a result of autoproteolysis at post-proline peptide bonds in the N-terminal parts of the molecules. Comparison of deduced amino acid sequences revealed a 94% similarity between S. oralis and S. mitis IgA1 proteases and a 75 to 79% similarity between IgA1 proteases of these species and those of S. pneumoniae and S. sanguis, respectively. Combined with the results of RFLP analyses using different iga gene fragments as probes, the results of nucleotide sequence comparisons provide evidence of horizontal transfer of iga gene sequences among individual strains of S. sanguis as well as among S. mitis and the two speciesS. pneumoniae and S. oralis. Whileiga genes of S. sanguis and S. oralis were highly homogeneous, the genes of S. pneumoniae and S. mitis showed extensive polymorphism reflected in different degrees of antigenic diversity.
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Purdy, Jay E., John E. Donelson, and Mary E. Wilson. "Regulation of genes encoding the major surface protease of Leishmania chagasi via mRNA stability." Molecular and Biochemical Parasitology 142, no. 1 (July 2005): 88–97. http://dx.doi.org/10.1016/j.molbiopara.2005.03.010.
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Waller, P. R., and R. T. Sauer. "Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease." Journal of bacteriology 178, no. 4 (1996): 1146–53. http://dx.doi.org/10.1128/jb.178.4.1146-1153.1996.
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Punt, Peter J., Frank H. J. Schuren, Jan Lehmbeck, Tove Christensen, Carsten Hjort, and Cees A. M. J. J. van den Hondel. "Characterization of the Aspergillus niger prtT, a unique regulator of extracellular protease encoding genes." Fungal Genetics and Biology 45, no. 12 (December 2008): 1591–99. http://dx.doi.org/10.1016/j.fgb.2008.09.007.
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Nakayama, Jiro, Reiko Kariyama, and Hiromi Kumon. "Description of a 23.9-Kilobase Chromosomal Deletion Containing a Region Encoding fsr Genes Which Mainly Determines the Gelatinase-Negative Phenotype of Clinical Isolates of Enterococcus faecalis in Urine." Applied and Environmental Microbiology 68, no. 6 (June 2002): 3152–55. http://dx.doi.org/10.1128/aem.68.6.3152-3155.2002.
Повний текст джерелаАнотація:
ABSTRACT Expression of virulence-related extracellular proteases, gelatinase, and serine protease of Enterococcus faecalis is regulated by a quorum-sensing system encoded by the fsr gene cluster. In this study, a 23.9-kb chromosomal deletion containing the fsr gene cluster region was found to be present in the majority (79%) of gelatinase-negative clinical isolates of E. faecalis from urine.
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Liao, Ching-Hsing, and Daniel E. McCallus. "Biochemical and Genetic Characterization of an Extracellular Protease from Pseudomonas fluorescensCY091." Applied and Environmental Microbiology 64, no. 3 (March 1, 1998): 914–21. http://dx.doi.org/10.1128/aem.64.3.914-921.1998.
Повний текст джерелаАнотація:
ABSTRACT Pseudomonas fluorescens CY091 cultures produce an extracellular protease with an estimated molecular mass of 50 kDa. Production of this enzyme (designated AprX) was observed in media containing CaCl2 or SrCl2 but not in media containing ZnCl2, MgCl2, or MnCl2. The requirement of Ca2+ (or Sr2+) for enzyme production was concentration dependent, and the optimal concentration for production was determined to be 0.35 mM. Following ammonium sulfate precipitation and ion-exchange chromatography, the AprX in the culture supernatant was purified to near electrophoretic homogeneity. Over 20% of the enzyme activity was retained in the AprX sample which had been heated in boiling water for 10 min, indicating that the enzyme is highly resistant to heat inactivation. The enzyme activity was almost completely inhibited in the presence of 1 mM 1,10-phenanthroline, but only 30% of the activity was inhibited in the presence of 1 mM EGTA. The gene encoding AprX was cloned from the genome of P. fluorescens CY091 by isolating cosmid clones capable of restoring the protease production in a nonproteolytic mutant of strain CY091. The genomic region of strain CY091 containing the aprX gene was located within a 7.3-kb DNA fragment. Analysis of the complete nucleotide sequence of this 7.3-kb fragment revealed the presence of a cluster of genes required for the production of extracellular AprX inP. fluorescens and Escherichia coli. The AprX protein showed 50 to 60% identity in amino acid sequence to the related proteases produced by Pseudomonas aeruginosa andErwinia chrysanthemi. Two conserved sequence domains possibly associated with Ca2+ and Zn2+ binding were identified. Immediately adjacent to the aprXstructural gene, a gene (inh) encoding a putative protease inhibitor and three genes (aprD, aprE, andaprF), possibly required for the transport of AprX, were also identified. The organization of the gene cluster involved in the synthesis and secretion of AprX in P. fluorescens CY091 appears to be somewhat different from that previously demonstrated inP. aeruginosa and E. chrysanthemi.
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Reithner, Barbara, Enrique Ibarra-Laclette, Robert L. Mach, and Alfredo Herrera-Estrella. "Identification of Mycoparasitism-Related Genes in Trichoderma atroviride." Applied and Environmental Microbiology 77, no. 13 (April 29, 2011): 4361–70. http://dx.doi.org/10.1128/aem.00129-11.
Повний текст джерелаАнотація:
ABSTRACTA high-throughput sequencing approach was utilized to carry out a comparative transcriptome analysis ofTrichoderma atrovirideIMI206040 during mycoparasitic interactions with the plant-pathogenic fungusRhizoctonia solani. In this study, transcript fragments of 7,797Trichodermagenes were sequenced, 175 of which were host responsive. According to the functional annotation of these genes by KOG (eukaryotic orthologous groups), the most abundant group during direct contact was “metabolism.” Quantitative reverse transcription (RT)-PCR confirmed the differential transcription of 13 genes (includingswo1, encoding an expansin-like protein;axe1, coding for an acetyl xylan esterase; and homologs of genes encoding the aspartyl proteasepapAand a trypsin-like protease,pra1) in the presence ofR. solani. An additional relative gene expression analysis of these genes, conducted at different stages of mycoparasitism againstBotrytis cinereaandPhytophthora capsici, revealed a synergistic transcription of various genes involved in cell wall degradation. The similarities in expression patterns and the occurrence of regulatory binding sites in the corresponding promoter regions suggest a possible analog regulation of these genes during the mycoparasitism ofT. atroviride. Furthermore, a chitin- and distance-dependent induction ofpra1was demonstrated.
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Savariau-Lacomme, Marie-Pierre, Carole Lebarbier, Tuomo Karjalainen, Anne Collignon, and Claire Janoir. "Transcription and Analysis of Polymorphism in a Cluster of Genes Encoding Surface-Associated Proteins of Clostridium difficile." Journal of Bacteriology 185, no. 15 (August 1, 2003): 4461–70. http://dx.doi.org/10.1128/jb.185.15.4461-4470.2003.
Повний текст джерелаАнотація:
ABSTRACT Recent investigations of the Clostridium difficile genome have revealed the presence of a cluster of 17 genes, 11 of which encode proteins with similar two-domain structures, likely to be surface-anchored proteins. Two of these genes have been proven to encode proteins involved in cell adherence: slpA encodes the precursor of the two proteins of the S-layer, P36 and P47, whereas cwp66 encodes the Cwp66 adhesin. To gain further insight into the function of this cluster, we further focused on slpA, cwp66, and cwp84, the latter of which encodes a putative surface-associated protein with homology to numerous cysteine proteases. It displayed nonspecific proteolytic activity when expressed as a recombinant protein in Escherichia coli. Polymorphism of cwp66 and cwp84 genes was analyzed in 28 strains, and transcriptional organization of the three genes was explored by Northern blots. The slpA gene is strongly transcribed during the entire growth phase as a bicistronic transcript; cwp66 is transcribed only in the early exponential growth phase as a polycistronic transcript encompassing the two contiguous genes upstream. The putative proteins encoded by the cotranscribed genes have no significant homology with known proteins but may have a role in adherence. No correlation could be established between sequence patterns of Cwp66 and Cwp84 and virulence of the strains. The cwp84 gene is strongly transcribed as a monocistronic message. This feature, together with the highly conserved sequence pattern of cwp84, suggests a significant role in the physiopathology of C. difficile for the Cwp84 protease, potentially in the maturation of surface-associated adhesins encoded by the gene cluster.
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Heusipp, Gerhard, Glenn M. Young, and Virginia L. Miller. "HreP, an In Vivo-Expressed Protease of Yersinia enterocolitica, Is a New Member of the Family of Subtilisin/Kexin-Like Proteases." Journal of Bacteriology 183, no. 12 (June 15, 2001): 3556–63. http://dx.doi.org/10.1128/jb.183.12.3556-3563.2001.
Повний текст джерелаАнотація:
ABSTRACT The role of proteases in pathogenesis is well established for several microorganisms but has not been described for Yersinia enterocolitica. Previously, we identified a gene,hreP, which showed significant similarity to proteases in a screen for chromosomal genes of Y. enterocoliticathat were exclusively expressed during an infection of mice. We cloned this gene by chromosome capture and subsequently determined its nucleotide sequence. Like inv, the gene encoding the invasin protein of Y. enterocolitica,hreP is located in a cluster of flagellum biosynthesis and chemotaxis genes. The genomic organization of this chromosomal region is different in Escherichia coli, Salmonella, andYersinia pestis than in Y. enterocolitica. Analysis of the distribution ofhreP between different Yersinia isolates and the relatively low G+C content of the gene suggests acquisition by horizontal gene transfer. Sequence analysis also revealed that HreP belongs to a family of eukaryotic subtilisin/kexin-like proteases. Together with the calcium-dependent protease PrcA of Anabaena variabilis, HreP forms a new subfamily of bacterial subtilisin/kexin-like proteases which might have originated from a common eukaryotic ancestor. Like other proteases of this family, HreP is expressed with an N-terminal prosequence. Expression of an HreP-His6 tag fusion protein in E. coli revealed that HreP undergoes autocatalytic processing at a consensus cleavage site of subtilisin/kexin-like proteases, thereby releasing the proprotein.
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BALASUBRAMANIAN, NATESAN, and NELSON SIMÕES. "Cloning and molecular analysis of the aspartic protease Sc-ASP110 gene transcript in Steinernema carpocapsae." Parasitology 140, no. 9 (June 4, 2013): 1158–67. http://dx.doi.org/10.1017/s0031182013000577.
Повний текст джерелаАнотація:
SUMMARYMany protease genes have previously been shown to be involved in parasitism and in the development of Steinernema carpocapsae, including a gene predicted to encode an aspartic protease, Sc-ASP110, which was cloned and was analysed in this study. A cDNA encoding Sc-ASP110 was cloned based on an expressed sequence tag (EST) fragment from our EST library. The full-length cDNA of Sc-ASP110 consists of 1112 nucleotides with a catalytic aspartic domain (aa18–337). The putative 341 amino acid residues have a calculated molecular mass of 37·1 kDa and a theoretical pI of 4·7. BLASTp analysis of the Sc-ASP110 amino acid sequence showed 45–77% amino acid sequence identity to parasitic and non-parasitic nematode aspartic proteases. An expression analysis showed that the sc-asp110 gene was upregulated during the late parasitic stage, L4, and 24 h after induction of in vitro nematodes. A sequence comparison revealed that Sc-ASP110 was a member of an aspartic protease family; additionally, a phylogenetic analysis indicated that Sc-ASP110 was clustered with the closely related nematode Steinernema feltiae. In situ hybridization showed that sc-asp110 was expressed in the body walls of dorsal cells. The upregulated Sc-ASP110 expression revealed that this protease could play a role in the late parasitic process. In this study, we have cloned and analysed the gene transcript of Sc-ASP110 in S. carpocapsae.