Journal articles: 'Pepy I'

1

Zhang, Huixin, Mengfan Xu, Shanhu Hu, Hongfei Zhao, and Bolin Zhang. "The Enzyme Gene Expression of Protein Utilization and Metabolism by Lactobacillus helveticus CICC 22171." Microorganisms 10, no. 9 (August 26, 2022): 1724. http://dx.doi.org/10.3390/microorganisms10091724.

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The purpose of this study was to explore the hydrolytic ability of Lactobacillus helveticus CICC 22171 with regard to protein and the expression of enzyme genes during protein utilization. The results revealed that the strain hydrolyzed casein from the C-terminal, reached the maximum level in 6 h, and the number of amino acids in the hydrolyzed peptide was 7–33. The molecular weight was 652.4–3432.74 kDa. Hydrophobic peptides produced by hydrolysis were the source of β-casein bitterness. Leucine and glutamine were the preferred cleavage points after 1 h; tyrosine and tryptophan subsequently increased. The first step of hydrolysis was controlled by PrtP and PrtM genes and coordinated with the action of PrtH1 and PrtH2. The transport system consisted of DtpT, OppB, OppD and OppF. The hydrolytic third step endopeptidase system consisted of the aminopeptidases (PepN, PepC, PepM and PepA), the endopeptidases (PepE, PepF and PepO); the dipeptidases (PepV and PepD), the tripeptidase PepT; the proline peptidases (PepX, PepP, PepQ, PepR and PepI). The expression of CEP genes was significantly different, and the expression level of genes related to the transport system significantly increased from 0 to 1 h. The specificity of the substrate and action site of endopeptidase was abundant.

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Guédon, Eric, Pierre Renault, S. Dusko Ehrlich, and Christine Delorme. "Transcriptional Pattern of Genes Coding for the Proteolytic System of Lactococcus lactis and Evidence for Coordinated Regulation of Key Enzymes by Peptide Supply." Journal of Bacteriology 183, no. 12 (June 15, 2001): 3614–22. http://dx.doi.org/10.1128/jb.183.12.3614-3622.2001.

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ABSTRACT The transcription of 16 genes encoding 12 peptidases (pepC, pepN, pepX, pepP, pepA, pepF2, pepDA1, pepDA2, pepQ, pepT, pepM, and pepO1), PI and PIII proteinases (prtP1 and prtP3), and three transport systems (dtpT, dtpP, and opp-pepO1) ofLactococcus lactis MG1363 was analyzed in response to different environmental factors. Promoter fusions with luciferase reporter genes and/or mRNA analysis were used to study the effects of sugar sources, growth at 37°C, and peptide supply on the transcription of these genes. Only transcription of thepepP gene is modulated by the source of sugar. The presence of potential catabolite-responsive element (CRE) boxes in its promoter region suggests that expression of this gene is directly controlled by catabolic repression. Elevated temperature had no significant effect on the level of transcription of these genes. prtP1, prtP3, pepC, pepN, pepX, and the opp-pepO1 operon are the most highly expressed genes in chemically defined medium, and their expression is repressed 5- to 150-fold by addition of peptide sources such as Casitone in the medium. Moreover, the transcription ofprtP1, prtP3, pepC, pepN, and the opp-pepO1operon is repressed two- to eight-fold by the dipeptides leucylproline and prolylleucine. The transcription of pepDA2 might also be repressed by the peptide sources, but this effect is not observed on the regulation of dtpT, pepP, pepA, pepF2, pepDA1, pepQ, pepT, pepM, and the dtpP operon. The significance of these results with respect to the functions of different components of the proteolytic system in L. lactis are discussed.

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Luoma, Susanna, Kirsi Peltoniemi, Vesa Joutsjoki, Terhi Rantanen, Marja Tamminen, Inka Heikkinen, and Airi Palva. "Expression of Six Peptidases fromLactobacillus helveticus in Lactococcus lactis." Applied and Environmental Microbiology 67, no. 3 (March 1, 2001): 1232–38. http://dx.doi.org/10.1128/aem.67.3.1232-1238.2001.

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ABSTRACT For development of novel starter strains with improved proteolytic properties, the ability of Lactococcus lactis to produceLactobacillus helveticus aminopeptidase N (PepN), aminopeptidase C (PepC), X-prolyl dipeptidyl aminopeptidase (PepX), proline iminopeptidase (PepI), prolinase (PepR), and dipeptidase (PepD) was studied by introducing the genes encoding these enzymes intoL. lactis MG1363 and its derivatives. According to Northern analyses and enzyme activity measurements, the L. helveticus aminopeptidase genes pepN, pepC, andpepX are expressed under the control of their own promoters in L. lactis. The highest expression level, using a low-copy-number vector, was obtained with the L. helveticus pepN gene, which resulted in a 25-fold increase in PepN activity compared to that of wild-type L. lactis. The L. helveticus pepI gene, residing as a third gene in an operon in its host, was expressed in L. lactis under the control of the L. helveticus pepX promoter. The genetic background of the L. lactis derivatives tested did not affect the expression level of any of the L. helveticus peptidases studied. However, the growth medium used affected both the recombinant peptidase profiles in transformant strains and the resident peptidase activities. The levels of expression of the L. helveticus pepD and pepR clones under the control of their own promoters were below the detection limit in L. lactis. However, substantial amounts of recombinant pepD and PepR activities were obtained in L. lactis when pepDand pepR were expressed under the control of the inducible lactococcal nisA promoter at an optimized nisin concentration.

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Vermeulen, Nicoline, Melanie Pavlovic, Matthias A. Ehrmann, Michael G. Gänzle, and Rudi F. Vogel. "Functional Characterization of the Proteolytic System of Lactobacillus sanfranciscensis DSM 20451T during Growth in Sourdough." Applied and Environmental Microbiology 71, no. 10 (October 2005): 6260–66. http://dx.doi.org/10.1128/aem.71.10.6260-6266.2005.

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ABSTRACT Protein hydrolysis and amino acid metabolism contribute to the beneficial effects of sourdough fermentation on bread quality. In this work, genes of Lactobacillus sanfranciscensis strain DSM 20451 involved in peptide uptake and hydrolysis were identified and their expression during growth in sourdough was determined. Screening of the L. sanfranciscensis genome with degenerate primers targeting prt and analysis of proteolytic activity in vitro provided no indication for proteolytic activity. Proteolysis in aseptic doughs and sourdoughs fermented with L. sanfranciscensis was inhibited upon the addition of an aspartic protease inhibitor. These results indicate that proteolysis was not linked to the presence of L. sanfranciscensis DSM 20451 and that this strain does not harbor a proteinase. Genes encoding the peptide transport systems Opp and DtpT and the intracellular peptidases PepT, PepR, PepC, PepN, and PepX were identified. Both peptide uptake systems and the genes pepN, pepX, pepC, and pepT were expressed by L. sanfranciscensis growing exponentially in sourdough, whereas pepX was not transcribed. The regulation of the expression of Opp, DtpT, and PepT during growth of L. sanfranciscensis in sourdough was investigated. Expression of Opp and DtpT was reduced approximately 17-fold when the peptide supply in dough was increased. The expression of PepT was dependent on the peptide supply to a lesser extent. Thus, the accumulation of amino nitrogen by L. sanfranciscensis in dough is attributable to peptide hydrolysis rather than proteolysis and amino acid metabolism by L. sanfranciscensis during growth in sourdough is limited by the peptide availability.

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Wegmann, U., J. R. Klein, I. Drumm, O. P. Kuipers, and B. Henrich. "Introduction of Peptidase Genes from Lactobacillus delbrueckii subsp. lactis into Lactococcus lactis and Controlled Expression." Applied and Environmental Microbiology 65, no. 11 (November 1, 1999): 4729–33. http://dx.doi.org/10.1128/aem.65.11.4729-4733.1999.

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ABSTRACT Peptidases PepI, PepL, PepW, and PepG from Lactobacillus delbrueckii subsp. lactis, which have no counterparts in Lactococcus lactis, and peptidase PepQ were examined to determine their potential to confer new peptidolytic properties to lactococci. Controllable expression of the corresponding genes (pep genes) was achieved by constructing translational fusions with the promoter of the nisA gene (P nisA ). A suitable host strain, UKLc10, was constructed by chromosomal integration of the genes encoding the NisRK two-component system into the fivefold peptidase-deficient mutant IM16 of L. lactis. Recombinants of this strain were used to analyze growth, peptidase activities, peptide utilization, and intracellular protein cleavage products. After nisin induction ofPnisA ::pep fusions, all of the peptidases were visible as distinct bands in protein gels. Despite the fact that identical transcription and translation signals were used to express the pep genes, the relative amounts of individual peptidases varied considerably. All of the peptidases exhibited activities in extracts of recombinant UKLc10 clones, but only PepL and PepG allowed the clones to utilize specific peptide substrates as sources of essential amino acids. In milk medium, induction ofpepG and induction of pepW resulted in growth acceleration. The activities of all five peptidases during growth in milk medium were revealed by high-performance liquid chromatography analyses of intracellular amino acid and peptide pools.

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Preston, R. A., P. S. Reinagel, and E. W. Jones. "Genes required for vacuolar acidity in Saccharomyces cerevisiae." Genetics 131, no. 3 (July 1, 1992): 551–58. http://dx.doi.org/10.1093/genetics/131.3.551.

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Abstract Mutations that cause loss of acidity in the vacuole (lysosome) of Saccharomyces cerevisiae were identified by screening colonies labeled with the fluorescent, pH-sensitive, vacuolar labeling agent, 6-carboxyfluorescein. Thirty nine vacuolar pH (Vph-) mutants were identified. Four of these contained mutant alleles of the previously described PEP3, PEP5, PEP6 and PEP7 genes. The remaining mutants defined eight complementation groups of vph mutations. No alleles of the VAT2 or TFP1 genes (known to encode subunits of the vacuolar H(+)-ATPase) were identified in the Vph- screen. Strains bearing mutations in any of six of the VPH genes failed to grow on medium buffered at neutral pH; otherwise, none of the vph mutations caused notable growth inhibition on standard yeast media. Expression of the vacuolar protease, carboxypeptidase Y, was defective in strains bearing vph4 mutations but was apparently normal in strains bearing any of the other vph mutations. Defects in vacuolar morphology at the light microscope level were evident in all Vph- mutants. Strains that contained representative mutant alleles of the 17 previously described PEP genes were assayed for vacuolar pH; mutations in seven of the PEP genes (including PEP3, PEP5, PEP6 and PEP7) caused loss of vacuolar acidity.

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Pag, Ulrike, Christoph Heidrich, Gabriele Bierbaum, and Hans-Georg Sahl. "Molecular Analysis of Expression of the Lantibiotic Pep5 Immunity Phenotype." Applied and Environmental Microbiology 65, no. 2 (February 1, 1999): 591–98. http://dx.doi.org/10.1128/aem.65.2.591-598.1999.

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ABSTRACT The lantibiotic Pep5 is produced by Staphylococcus epidermidis 5. Within its biosynthetic gene cluster, the immunity gene pepI, providing producer self-protection, is localized upstream of the structural gene pepA. Pep5 production and the immunity phenotype have been found to be tightly coupled (M. Reis, M. Eschbach-Bludau, M. I. Iglesias-Wind, T. Kupke, and H.-G. Sahl, Appl. Environ. Microbiol. 60:2876–2883, 1994). To study this phenomenon, we analyzed pepA and pepItranscription and translation and constructed a number of strains containing various fragments of the gene cluster and expressing different levels of immunity. Complementation of apepA-expressing strain with pepI intrans did not result in phenotypic immunity or production of PepI. On the other hand, neither pepA nor its product was found to be involved in immunity, since suppression of the translation of the pepA mRNA by mutation of the ATG start codon did not reduce the level of immunity. Moreover, homologous and heterologous expression of pepI from a xylose-inducible promoter resulted in significant Pep5 insensitivity. Most important for expression of the immunity phenotype was the stability ofpepI transcripts, which in the wild-type strain, is achieved by an inverted repeat with a free energy of −56.9 kJ/mol, localized downstream of pepA. We performed site-directed mutagenesis to study the functional role of PepI and constructed F13D PepI, I17R PepI, and PepI 1-65; all mutants showed reduced levels of immunity. Western blot analysis indicated that F13D PepI and PepI 1-65 were not produced correctly or were partially degraded, while I17R PepI apparently was less efficient in providing self-protection than the wild-type PepI.

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8

Fischer, Henry G. "The Transcription of the Royal Name Pepy." Journal of Egyptian Archaeology 75 (1989): 214. http://dx.doi.org/10.2307/3821910.

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Fischer, Henry G. "The Transcription of the Royal Name Pepy." Journal of Egyptian Archaeology 75, no. 1 (August 1989): 214–15. http://dx.doi.org/10.1177/030751338907500117.

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10

Chandu, Dilip, and Dipankar Nandi. "PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress." Microbiology 149, no. 12 (December 1, 2003): 3437–47. http://dx.doi.org/10.1099/mic.0.26518-0.

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PepN and its homologues are involved in the ATP-independent steps (downstream processing) during cytosolic protein degradation. To obtain insights into the contribution of PepN to the peptidase activity in Escherichia coli, the hydrolysis of a selection of endopeptidase and exopeptidase substrates was studied in extracts of wild-type strains and two pepN mutants, 9218 and DH5αΔpepN. Hydrolysis of three of the seven endopeptidase substrates tested was reduced in both pepN mutants. Similar studies revealed that hydrolysis of 10 of 14 exopeptidase substrates studied was greatly reduced in both pepN mutants. This decreased ability to cleave these substrates is pepN-specific as there is no reduction in the ability to hydrolyse exopeptidase substrates in E. coli mutants lacking other peptidases, pepA, pepB or pepE. PepN overexpression complemented the hydrolysis of the affected exopeptidase substrates. These results suggest that PepN is responsible for the majority of aminopeptidase activity in E. coli. Further in vitro studies with purified PepN revealed a preference to cleave basic and small amino acids as aminopeptidase substrates. Kinetic characterization revealed the aminopeptidase cleavage preference of E. coli PepN to be Arg>Ala>Lys>Gly. Finally, it was shown that PepN is a negative regulator of the sodium-salicylate-induced stress in E. coli, demonstrating a physiological role for this aminoendopeptidase under some stress conditions.

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Laan, Harry, Roel E. Haverkort, Loe De Leij, and Wil N. Konings. "Detection and localization of peptidases inLactococcus lactiswith monoclonal antibodies." Journal of Dairy Research 63, no. 2 (May 1996): 245–56. http://dx.doi.org/10.1017/s0022029900031745.

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SummaryMonoclonal antibodies against peptidases ofLactococcus lactiswere isolated and characterized: PEPN1–4 against a lysyl aminopeptidase PepN, PEPT1–5 against a tripeptidase PepT and PEPD1–3 against a dipeptidase PepD. These monoclonal antibodies reacted specifically with their respective antigens in crude cell extracts ofLc. lactissubspp.cremorisandlactis. A number of monoclonal antibodies cross reacted with proteins of other (lactic acid) bacteria. PEPT1, 2, 4 and 5 cross reacted weakly with a 35 kDa protein inLactobacillus delbrueckii, while PEPT1 and PEPT2 reacted with proteins in the cell-free extract ofStreptococcus thermophilusandClostridium fervidus. Of the four isolated monoclonal antibodies against PepN, only PEPN3 cross reacted weakly with a 90 kDa protein inEscherichia colicell-free extract, and the other three antibody species against PepN cross reacted with 80 kDa proteins ofLb. casei, Lb. delbrueckii, andStr. bovis, but not ofEsch. coli. Of the three monoclonal antibodies against PepD, only PEPD1 and PEPD2 cross reacted with 40 kDa proteins ofLb. casei, Lb. delbrueckiiandStr. bovis. All PEPN, PEPD and PEPT antibodies reacted with components in cell-free extracts of eleven differentLc. lactisstrains, indicating that the peptidases of these strains were very similar to those ofLc. lactissubsp.cremorisWG2. However,Lc. lactissubsp.hordniaeappeared to differ from the otherLc. lactissubspecies since only PEPT1, 2 and 5 reacted with a protein in the cell-free extract. Immunogold labelling ofLc. lactisWG2 with the isolated monoclonal antibodies revealed that PepN, PepD and PepT were located intracellularly. The intracellular location of these peptidases is discussed in relation to the supply of essential amino acids and peptides.

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Droppa-Almeida, Daniela, Glenda Amaral da Silva, Lívia Maria do Amorim Costa Gaspar, Beatriz Benny Sungaila Pereyra, Roberto José Meyer Nascimento, Sibele Borsuk, Elton Franceschi, and Francine Ferreira Padilha. "Peptide vaccines designed with the aid of immunoinformatic against Caseous Lymphadenitis promotes humoral and cellular response induction in mice." PLOS ONE 16, no. 11 (November 29, 2021): e0256864. http://dx.doi.org/10.1371/journal.pone.0256864.

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Caseous Lymphadenitis (CLA) is a chronic disease that affects also small ruminants. CLA is caused by Corynebacterium pseudotuberculosis and is responsible for high economic losses due to the formation of superficial and visceral granulomas, the latter is considered as asymptomatic CLA causing high levels of dissemination. Several vaccination strategies, in which the use of synthetic peptides stands out. Thus, this work aimed to evaluate the protective potential of peptide vaccines designed to determine the immunodominant epitopes of CP40 against CLA in mice. The animals were divided into eight groups separated in controls (G1—PBS, G2—Saponin and G9—rCP40) and experimental (G3—pep1, G4- pep2, G5-pep3, G6-pep4, G7-pep5 and G8-pep6), these were vaccinated on days 0 and 15 by a subcutaneous route. 60 days after the first immunization, all animals were challenged with C. pseudotuberculosis. On days 0, 15, 60, and 120 after the first immunization, blood samples were taken to measure immunoglobulins. On the same day of the challenge, the splenocytes were isolated and assayed for the production of IL-2, IL-4, IL-6, IFN-γ, TNF-α, IL-17, and IL-10. After vaccinations, the animals were challenged and all of them were affected by the disease which led to their death. The G6 and G8 groups provided 10% protection and the G7 provided 20%. The G3 and G4 groups provided 30% and 40% protection respectively. The peptides showed the production of Total IgG antibodies and cytokines (IL-2, IL-4, IL-6, IFN-γ, and TNF-α), indicating a possible activation of the Th1 type response. However, groups G3, G5, G6, and G8 showed production of IL-17. None of the study groups showed IL-10 production. The immunogenicity of the peptides was not enough to protect these animals and it is believed that the use of adjuvants based on PAMPs may improve the immune response offered by these peptides.

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Aparin, Ilya O., Valentina M. Farzan, Olga A. Veselova, Alexey A. Chistov, Alexander T. Podkolzin, Alexey V. Ustinov, German A. Shipulin, Andrey A. Formanovsky, Vladimir A. Korshun, and Timofei S. Zatsepin. "1-Phenylethynylpyrene (PEPy) as a novel blue-emitting dye for qPCR assay." Analyst 141, no. 4 (2016): 1331–38. http://dx.doi.org/10.1039/c5an01767j.

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We demonstrated that 1-phenylethynylpyrene (PEPy) is a superior substitute for AMCA and Alexa-350 as a short wavelength fluorescent dye for end-point PCR and quantitative PCR. This study broadens the panel of fluorescent dyes suitable for the use in Taqman probes.

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Merfa, Marcus Vinícius, Eduarda Regina Fischer, Mariana de Souza e Silva, Carolina Sardinha Francisco, Helvécio Della Coletta-Filho, and Alessandra Alves de Souza. "Probing the Application of OmpA-Derived Peptides to Disrupt the Acquisition of ‘Candidatus Liberibacter asiaticus’ by Diaphorina citri." Phytopathology® 112, no. 1 (January 2022): 163–72. http://dx.doi.org/10.1094/phyto-06-21-0252-fi.

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Huanglongbing (HLB) is currently the most devastating disease of citrus worldwide. Both bacteria ‘Candidatus Liberibacter asiaticus’ (CLas) and ‘Candidatus Liberibacter americanus’ (CLam) are associated with HLB in Brazil but with a strong prevalence of CLas over CLam. Conventionally, HLB management focuses on controlling the insect vector population (Diaphorina citri; also known as Asian citrus psyllid [ACP]) by spraying insecticides, an approach demonstrated to be mostly ineffective. Thus, development of novel, more efficient HLB control strategies is required. The multifunctional bacterial outer membrane protein OmpA is involved in several molecular processes between bacteria and their hosts and has been suggested as a target for bacterial control. Curiously, OmpA is absent in CLam in comparison with CLas, suggesting a possible role in host interaction. Therefore, in the current study, we have treated ACPs with different OmpA-derived peptides, aiming to evaluate acquisition of CLas by the insect vector. Treatment of psyllids with 5 µM of Pep1, Pep3, Pep5, and Pep6 in artificial diet significantly reduced the acquisition of CLas, whereas increasing the concentration of Pep5 and Pep6 to 50 µM abolished this process. In addition, in planta treatment with 50 µM of Pep6 also significantly decreased the acquisition of CLas, and sweet orange plants stably absorbed and maintained this peptide for as long as 3 months post the final application. Together, our results demonstrate the promising use of OmpA-derived peptides as a novel biotechnological tool to control CLas.

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Do Carmo, A., D. da Silva, M. De Oliveira, A. Borges, A. De Carvalho, and C. De Moraes. "Genes involved in protein metabolism of the probiotic lactic acid bacterium Lactobacillus delbrueckii UFV H2b20." Beneficial Microbes 2, no. 3 (September 1, 2011): 209–20. http://dx.doi.org/10.3920/bm2011.0025.

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A basic requirement for the prediction of the potential use of lactic acid bacteria (LAB) in the dairy industry is the identification of specific genes involved in flavour-forming pathways. The probiotic Lactobacillus delbrueckii UFV H2b20 was submitted to a genetic characterisation and phylogenetic analysis of genes involved in protein catabolism. Eight genes belonging to this system were identified, which possess a closely phylogenetic relationship to NCFM strains representative, as it was demonstrated for oppC and oppBII, encoding oligopeptide transport system components. PepC, PepN, and PepX might be essential for growth of LAB, probiotic or not, since the correspondent genes are always present, including in L. delbrueckii UFV H2b20 genome. For pepX gene, a probable link between carbohydrate catabolism and PepX expression may exists, where it is regulated by PepR1/CcpA-like, a common feature between Lactobacillus strains and also in L. delbrueckii UFV H2b20. The well conserved evolutionary history of the ilvE gene is evidence that the pathways leading to branched-chain amino acid degradation, such as isoleucine and valine, are similar among L. delbrueckii subsp. bulgaricus strains and L. delbrueckii UFV H2b20. Thus, the involvement of succinate in flavour formation can be attributed to IlvE activity. The presence of aminopeptidase G in L. delbrueckii UFV H2b20 genome, which is absent in several strains, might improve the proteolytic activity and effectiveness. The nucleotide sequence encoding PepG revealed that it is a cysteine endopeptidase, belonging to Peptidase C1 superfamily; sequence analysis showed 99% identity with L. delbrueckii subsp. bulgaricus ATCC 11842 pepG, whereas protein sequence analysis revealed 100% similarity with PepG from the same organism. The present study proposes a schematic model to explain how the proteolytic system of the probiotic L. delbrueckii UFV H2b20 works, based on the components identified so far.

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Silva, Rúben D. M., João Franco Machado, Kyle Gonçalves, Francisco M. Lucas, Salete Batista, Rita Melo, Tânia S. Morais, and João D. G. Correia. "Ultrasonication Improves Solid Phase Synthesis of Peptides Specific for Fibroblast Growth Factor Receptor and for the Protein-Protein Interface RANK-TRAF6." Molecules 26, no. 23 (December 3, 2021): 7349. http://dx.doi.org/10.3390/molecules26237349.

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Considering our interest in the use of peptides as potential target-specific drugs or as delivery vectors of metallodrugs for various biomedical applications, it is crucial to explore improved synthetic methodologies to accomplish the highest peptide crude purity in the shortest time possible. Therefore, we compared “classical” fluorenylmethoxycarbonyl (Fmoc)-solid phase peptide synthesis (SPPS) with ultrasound(US)-assisted SPPS based on the preparation of three peptides, namely the fibroblast growth factor receptor 3(FGFR3)-specific peptide Pep1 (VSPPLTLGQLLS-NH2) and the novel peptides Pep2 (RQMATADEA-NH2) and Pep3 (AAVALLPAVLLALLAPRQMATADEA-NH2), which are being developed aimed at interfering with the intracellular protein-protein interaction(PPI) RANK-TRAF6. Our results demonstrated that US-assisted SPPS led to a 14-fold (Pep1) and 4-fold time reduction (Pep2) in peptide assembly compared to the “classical” method. Interestingly, US-assisted SPPS yielded Pep1 in higher purity (82%) than the “classical” SPPS (73%). The significant time reduction combined with high crude peptide purity attained prompted use to apply US-assisted SPPS to the large peptide Pep3, which displays a high number of hydrophobic amino acids and homooligo-sequences. Remarkably, the synthesis of this 25-mer peptide was attained during a “working day” (347 min) in moderate purity (approx. 49%). In conclusion, we have reinforced the importance of using US-SPPS towards facilitating the production of peptides in shorter time with increased efficacy in moderate to high crude purity. This is of special importance for long peptides such as the case of Pep3.

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Strudwick, Nigel. "Book Review: Balat, IV. Le Monument Funéraire D'Ima-Pepy/Ima-Meryrê." Journal of Egyptian Archaeology 91, no. 1 (December 2005): 204–5. http://dx.doi.org/10.1177/030751330509100119.

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De Angelis, Maria, Sonya Siragusa, Mirco Vacca, Raffaella Di Cagno, Fernanda Cristofori, Michael Schwarm, Stefan Pelzer, et al. "Selection of Gut-Resistant Bacteria and Construction of Microbial Consortia for Improving Gluten Digestion under Simulated Gastrointestinal Conditions." Nutrients 13, no. 3 (March 19, 2021): 992. http://dx.doi.org/10.3390/nu13030992.

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This work aimed to define the microbial consortia that are able to digest gluten into non-toxic and non-immunogenic peptides in the human gastrointestinal tract. Methods: 131 out of 504 tested Bacillus and lactic acid bacteria, specifically Bacillus (64), lactobacilli (63), Pediococcus (1), and Weissella (3), showed strong gastrointestinal resistance and were selected for their PepN, PepI, PepX, PepO, and PepP activities toward synthetic substrates. Based on multivariate analysis, 24 strains were clearly distinct from the other tested strains based on having the highest enzymatic activities. As estimated by RP-HPLC and nano-ESI–MS/MS, 6 cytoplasmic extracts out of 24 selected strains showed the ability to hydrolyze immunogenic epitopes, specifically 57–68 of α9-gliadin, 62–75 of A-gliadin, 134–153 of γ-gliadin, and 57–89 (33-mer) of α2-gliadin. Live and lysed cells of selected strains were combined into different microbial consortia for hydrolyzing gluten under gastrointestinal conditions. Commercial proteolytic enzymes (Aspergillusoryzae E1, Aspergillusniger E2, Bacillussubtilis Veron HPP, and Veron PS proteases) were also added to each microbial consortium. Consortium activity was evaluated by ELISA tests, RP-HPLC-nano-ESI–MS/MS, and duodenal explants from celiac disease patients. Results: two microbial consortia (Consortium 4: Lactiplantibacillus (Lp.) plantarum DSM33363 and DSM33364, Lacticaseibacillus (Lc.) paracasei DSM33373, Bacillussubtilis DSM33298, and Bacilluspumilus DSM33301; and Consortium 16: Lp. plantarum DSM33363 and DSM33364, Lc. paracasei DSM33373, Limosilactobacillusreuteri DSM33374, Bacillusmegaterium DSM33300, B.pumilus DSM33297 and DSM33355), containing commercial enzymes, were able to hydrolyze gluten to non-toxic and non-immunogenic peptides under gastrointestinal conditions. Conclusions: the results of this study provide evidence that selected microbial consortia could potentially improve the digestion of gluten in gluten-sensitive patients by hydrolyzing the immunogenic peptides during gastrointestinal digestion.

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Darnell, John Coleman. "The Chief Baker." Journal of Egyptian Archaeology 75, no. 1 (August 1989): 216–19. http://dx.doi.org/10.1177/030751338907500118.

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The previously misunderstood titles of the man Pepy on stele CG 20683 = ANOC 1:5 provide the earliest attestation for the word 'mr (Wb. 1, 187, 2), ‘bakery’ (cf. demotic 'mre and Coptic αMPε, ‘baker’). The titles also yield a Middle Kingdom example of the feminine form of šn' (Wb. iv, 507, 12–508, 25), ‘Workhouse’; a second Middle Kingdom survival of the Old Kingdom title imy-r 'bw-rȝ nsw.t, ‘Overseer of the Royal Repast’, is found among the titles of Iykhernofret on the stele.

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Sridhar, Vidya R., Joanne E. Hughes, Dennis L. Welker, Jeffery R. Broadbent, and James L. Steele. "Identification of Endopeptidase Genes from the Genomic Sequence of Lactobacillus helveticus CNRZ32 and the Role of These Genes in Hydrolysis of Model Bitter Peptides." Applied and Environmental Microbiology 71, no. 6 (June 2005): 3025–32. http://dx.doi.org/10.1128/aem.71.6.3025-3032.2005.

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ABSTRACT Genes encoding three putative endopeptidases were identified from a draft-quality genome sequence of Lactobacillus helveticus CNRZ32 and designated pepO3, pepF, and pepE2. The ability of cell extracts from Escherichia coli DH5α derivatives expressing CNRZ32 endopeptidases PepE, PepE2, PepF, PepO, PepO2, and PepO3 to hydrolyze the model bitter peptides, β-casein (β-CN) (f193-209) and αS1-casein (αS1-CN) (f1-9), under cheese-ripening conditions (pH 5.1, 4% NaCl, and 10°C) was examined. CNRZ32 PepO3 was determined to be a functional paralog of PepO2 and hydrolyzed both peptides, while PepE and PepF had unique specificities towards αS1-CN (f1-9) and β-CN (f193-209), respectively. CNRZ32 PepE2 and PepO did not hydrolyze either peptide under these conditions. To demonstrate the utility of these peptidases in cheese, PepE, PepO2, and PepO3 were expressed in Lactococcus lactis, a common cheese starter, using a high-copy vector pTRKH2 and under the control of the pepO3 promoter. Cell extracts of L. lactis derivatives expressing these peptidases were used to hydrolyze β-CN (f193-209) and αS1-CN (f1-9) under cheese-ripening conditions in single-peptide reactions, in a defined peptide mix, and in Cheddar cheese serum. Peptides αS1-CN (f1-9), αS1-CN (f1-13), and αS1-CN (f1-16) were identified from Cheddar cheese serum and included in the defined peptide mix. Our results demonstrate that in all systems examined, PepO2 and PepO3 had the highest activity with β-CN (f193-209) and αS1-CN (f1-9). Cheese-derived peptides were observed to affect the activity of some of the enzymes examined, underscoring the importance of incorporating such peptides in model systems. These data indicate that L. helveticus CNRZ32 endopeptidases PepO2 and PepO3 are likely to play a key role in this strain's ability to reduce bitterness in cheese.

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Sameh Shafik, Sameh. "The provincial policies of Teti, Pepy I and Merenre in Upper Egypt." International Journal of Heritage, Tourism and Hospitality 14, no. 2 (December 1, 2020): 61–72. http://dx.doi.org/10.21608/ijhth.2020.154172.

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Delmaire, Danielle. "Discours de Guillaume Pepy, président de la SNCF Bobigny 25 janvier 2011." Tsafon, no. 83 (June 15, 2022): 15–24. http://dx.doi.org/10.4000/tsafon.4664.

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23

Zhu, Aijun, Xukui Wang, Meixiang Yu, Ji-Quan Wang, and Anna-Liisa Brownell. "Evaluation of Four Pyridine Analogs to Characterize 6-OHDA-Induced Modulation of mGluR5 Function in Rat Brain Using microPET Studies." Journal of Cerebral Blood Flow & Metabolism 27, no. 9 (February 14, 2007): 1623–31. http://dx.doi.org/10.1038/sj.jcbfm.9600461.

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Micro-positron emission tomography imaging studies were conducted to characterize modulation of metabotropic glutamate subtype-5 receptor (mGluR5) function in a 6-hydroxydopamine (6-OHDA)-induced rat model of Parkinson's disease using four analogical PET ligands: 2-[11C]methyl-6-(2-phenylethynyl) pyridine ([11C]MPEP), 2-(2-(3-[11C]methoxyphenyl)ethynyl)pyridine ([11C]M-MPEP), 2-(2-(5-[11C]methoxypyridin-3-yl)ethynyl)pyridine ([11C]M-PEPy), and 3-[(2-[18F]methyl-1,3-thiazol-4-yl)ethynyl]pyridine ([18F]M-TEP). A total of 45 positron emission tomography (PET) imaging studies were conducted on nine male Sprague-Dawley rats within 4 to 6 weeks after unilateral 6-OHDA lesioning into the right medial forebrain bundle. The severity of the lesion was determined with [11C]CFT ([11C]2-β-carbomethoxy-3-β-(4-fluorophenyl)tropane), a specific and sensitive ligand for imaging dopamine transporter function. The binding potential (BP) images were processed on pixel-by-pixel basis by using a method of the distribution volume ratio with cerebellum as a reference tissue. The values for BP were determined on striatum, hippocampus, and cortex. [11C]CFT binding was decreased on the lesioned (right) striatum by 35.4% ± 13.4% compared with the intact left striatum, indicating corresponding loss of presynaptic dopamine terminals. On the same areas of the lesioned striatum, three of the four tested mGluR5 ligands showed enhanced binding characteristics. The average differences between the right and left striatum were 4.4% ± 6.5% ( P < 0.05) with [11C]MPEP, 0.1% ± 1.7% ( P > 0.05) with [11C]M-MPEP, 3.9% ± 4.6% ( P < 0.05) with [11C]M-PEPy, and 6.6% ± 2.7% ( P > 0.05) with [18F]M-TEP. The enhanced binding was also observed in the right hippocampus and cortex. These studies showed that glutamatergic neurotransmission might have a complementary role in dopaminergic degeneration, which can be evaluated by in vivo PET imaging.

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Kazakov, Teymur, Gaston H. Vondenhoff, Kirill A. Datsenko, Maria Novikova, Anastasia Metlitskaya, Barry L. Wanner, and Konstantin Severinov. "Escherichia coli Peptidase A, B, or N Can Process Translation Inhibitor Microcin C." Journal of Bacteriology 190, no. 7 (January 25, 2008): 2607–10. http://dx.doi.org/10.1128/jb.01956-07.

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ABSTRACT The heptapeptide-nucleotide microcin C (McC) targets aspartyl-tRNA synthetase. Upon its entry into a susceptible cell, McC is processed to release a nonhydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase, leading to the cessation of translation and cell growth. Here, we surveyed Escherichia coli cells with singly, doubly, and triply disrupted broad-specificity peptidase genes to show that any of three nonspecific oligopeptidases (PepA, PepB, or PepN) can effectively process McC. We also show that the rate-limiting step of McC processing in vitro is deformylation of the first methionine residue of McC.

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25

Soleiman, Saleh. "The Dating of Heneni’s False Door at Hildesheim." Journal of the American Research Center in Egypt 56, no. 1 (December 2020): 199–211. http://dx.doi.org/10.5913/jarce.56.2020.a013.

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This article deals with dating the false door of Heneni which was found at Giza and is now preserved in the Roemer-und Pelizaeus-Museum, Hildesheim. The false door is dated from late in the reign of Pepy II to the Eighth Dynasty on the basis of the place of its discovery in the cemetery, the name of its owner, the titles and epithets of the deceased, the prt-xrw formula, and its form and decoration. The small size and location of Heneni’s tomb are discussed. His rank and status are determined, the short offering formula on the false door is explicated, and a new reading and translation are suggested for the prt-xrw formula.

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26

Tabata, Kazuhiko, and Shin-ichi Hashimoto. "Fermentative Production of l-Alanyl-l-Glutamine by a Metabolically Engineered Escherichia coli Strain Expressing l-Amino Acid α-Ligase." Applied and Environmental Microbiology 73, no. 20 (August 24, 2007): 6378–85. http://dx.doi.org/10.1128/aem.01249-07.

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ABSTRACT In spite of its clinical and nutritional importance, l-alanyl-l-glutamine (Ala-Gln) has not been widely used due to the absence of an efficient manufacturing method. Here, we present a novel method for the fermentative production of Ala-Gln using an Escherichia coli strain expressing l-amino acid α-ligase (Lal), which catalyzes the formation of dipeptides by combining two amino acids in an ATP-dependent manner. Two metabolic manipulations were necessary for the production of Ala-Gln: reduction of dipeptide-degrading activity by combinatorial disruption of the dpp and pep genes and enhancement of the supply of substrate amino acids by deregulation of glutamine biosynthesis and overexpression of heterologous l-alanine dehydrogenase (Ald). Since expression of Lal was found to hamper cell growth, it was controlled using a stationary-phase-specific promoter. The final strain constructed was designated JKYPQ3 (pepA pepB pepD pepN dpp glnE glnB putA) containing pPE167 (lal and ald expressed under the control of the uspA promoter) or pPE177 (lal and ald expressed under the control of the rpoH promoter). Either strain produced more than 100 mM Ala-Gln extracellularly, in fed-batch cultivation on glucose-ammonium salt medium, without added alanine and glutamine. Because of the characteristics of Lal, no longer peptides (such as tripeptides) or dipeptides containing d-amino acids were formed.

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Astakhova, Irina V., Andrei D. Malakhov, Irina A. Stepanova, Alexey V. Ustinov, Stanislav L. Bondarev, Alexander S. Paramonov, and Vladimir A. Korshun. "1-Phenylethynylpyrene (1-PEPy) as Refined Excimer Forming Alternative to Pyrene: Case of DNA Major Groove Excimer." Bioconjugate Chemistry 18, no. 6 (November 2007): 1972–80. http://dx.doi.org/10.1021/bc700280h.

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28

Srivastava, Amit, Carol A. Woolford, and Elizabeth W. Jones. "Pep3p/Pep5p Complex: A Putative Docking Factor at Multiple Steps of Vesicular Transport to the Vacuole of Saccharomyces cerevisiae." Genetics 156, no. 1 (September 1, 2000): 105–22. http://dx.doi.org/10.1093/genetics/156.1.105.

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Abstract Pep3p and Pep5p are known to be necessary for trafficking of hydrolase precursors to the vacuole and for vacuolar biogenesis. These proteins are present in a hetero-oligomeric complex that mediates transport at the vacuolar membrane. PEP5 interacts genetically with VPS8, implicating Pep5p in the earlier Golgi to endosome step and/or in recycling from the endosome to the Golgi. To understand further the cellular roles of Pep3p and Pep5p, we isolated and characterized a set of pep3 conditional mutants. Characterization of mutants revealed that pep3ts mutants are defective in the endosomal and nonendosomal Golgi to vacuole transport pathways, in the cytoplasm to vacuole targeting pathway, in recycling from the endosome back to the late Golgi, and in endocytosis. PEP3 interacts genetically with two members of the endosomal SNARE complex, PEP12 (t-SNARE) and PEP7 (homologue of mammalian EEA1); Pep3p and Pep5p associate physically with Pep7p as revealed by two-hybrid analysis. Our results suggest that a core Pep3p/Pep5p complex promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole. We propose that this complex may be responsible for tethering transport vesicles on target membranes.

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29

Matos, J., M. Nardi, H. Kumura, and V. Monnet. "Genetic Characterization of pepP, Which Encodes an Aminopeptidase P Whose Deficiency Does Not AffectLactococcus lactis Growth in Milk, Unlike Deficiency of the X-Prolyl Dipeptidyl Aminopeptidase." Applied and Environmental Microbiology 64, no. 11 (November 1, 1998): 4591–95. http://dx.doi.org/10.1128/aem.64.11.4591-4595.1998.

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ABSTRACT We sequenced the pepP gene of Lactococcus lactis, which encodes an aminopeptidase P (PepP), and demonstrated that the X-prolyl dipeptidyl aminopeptidase PepX plays a more important role than PepP in nitrogen nutrition. PepP shares homology with methionine aminopeptidases and could play a role in the maturation of nascent proteins.

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30

Soeryapranata, Elly, Joseph R. Powers, and Gülhan Ünlü. "Cloning and characterization of debittering peptidases, PepE, PepO, PepO2, PepO3, and PepN, of Lactobacillus helveticus WSU19." International Dairy Journal 17, no. 9 (September 2007): 1096–106. http://dx.doi.org/10.1016/j.idairyj.2007.02.002.

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31

Koeda, Sota, Mika Onouchi, Namiko Mori, Nadya Syafira Pohan, Atsushi J. Nagano, and Elly Kesumawati. "A recessive gene pepy-1 encoding Pelota confers resistance to begomovirus isolates of PepYLCIV and PepYLCAV in Capsicum annuum." Theoretical and Applied Genetics 134, no. 9 (June 3, 2021): 2947–64. http://dx.doi.org/10.1007/s00122-021-03870-7.

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32

Cosford, Nicholas D. P., Jeffrey Roppe, Lida Tehrani, Edwin J. Schweiger, T. Jon Seiders, Ashok Chaudary, Sara Rao, and Mark A. Varney. "[3H]-Methoxymethyl-MTEP and [3H]-Methoxy-PEPy: potent and selective radioligands for the metabotropic glutamate subtype 5 (mGlu5) receptor." Bioorganic & Medicinal Chemistry Letters 13, no. 3 (February 2003): 351–54. http://dx.doi.org/10.1016/s0960-894x(02)00997-6.

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33

Hauser, Alan R., Suzanne Fleiszig, Pil Jung Kang, Keith Mostov, and Joanne N. Engel. "Defects in Type III Secretion Correlate with Internalization of Pseudomonas aeruginosa by Epithelial Cells." Infection and Immunity 66, no. 4 (April 1, 1998): 1413–20. http://dx.doi.org/10.1128/iai.66.4.1413-1420.1998.

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ABSTRACT Previous characterization of Pseudomonas aeruginosaclinical isolates has demonstrated an inverse correlation between cytotoxicity and internalization by epithelial cells. To further investigate this relationship, we tested PA103, a cytotoxicP. aeruginosa strain, and 33 isogenic noncytotoxic transposon mutants for internalization by Madin-Darby canine kidney cells. The majority of the mutants were not internalized, demonstrating that an inverse correlation between cytotoxicity and bacterial uptake by epithelial cells is not absolute. Six of the noncytotoxic mutants, however, demonstrated measurable levels of internalization by standard aminoglycoside exclusion assays even though internalization of wild-type strain PA103 was not detectable. All six had evidence of protein secretion defects involving two proteins, a 40-kDa protein and a 32-kDa protein. These proteins, designated PepB (forPseudomonas exoprotein B) and PepD, respectively, each had characteristics of type III transported proteins. In addition, nucleotide sequencing studies demonstrated that PepB and PepD are homologs of YopB and YopD, respectively, type III secreted proteins ofYersinia spp. necessary for the translocation of effector molecules into the cytoplasmic compartment of eukaryotic cells. Thus, while many mutations in PA103 result in loss of cytotoxicity without an appreciable increase in internalization, defects in transport of type III secretion proteins PepB and PepD correlate with both loss of cytotoxicity and gain of internalization. These results are consistent with type III secretion of an inhibitor of internalization that requires PepB and PepD for translocation into the host cell.

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Hoffmann, Anja, Tanja Schneider, Ulrike Pag, and Hans-Georg Sahl. "Localization and Functional Analysis of PepI, the Immunity Peptide of Pep5-Producing Staphylococcus epidermidis Strain 5." Applied and Environmental Microbiology 70, no. 6 (June 2004): 3263–71. http://dx.doi.org/10.1128/aem.70.6.3263-3271.2004.

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ABSTRACT Pep5 is a cationic pore-forming lantibiotic produced by Staphylococcus epidermidis strain 5. The producer strain protects itself from the lethal action of its own bacteriocin through the 69-amino-acid immunity peptide PepI. The N-terminal segment of PepI contains a 20-amino-acid stretch of apolar residues, whereas the C terminus is very hydrophilic, with a net positive charge. We used green fluorescent protein (GFP)-PepI fusions to obtain information on its localization in vivo. PepI was found to occur outside the cytoplasm and to accumulate at the membrane-cell wall interface. The extracellular localization appeared essential for conferring immunity. We analyzed the functional role of the specific segments by constructing various mutant peptides, which were also fused to GFP. When the hydrophobic N-terminal segment of PepI was disrupted by introducing charged amino acids, the export of PepI was blocked and clones expressing such mutant peptides were Pep5 sensitive. When PepI was successively shortened at the C terminus, in contrast, its export properties remained unchanged whereas its ability to confer immunity was gradually reduced. The results show that the N-terminal part is required for the transport of PepI and that the C-terminal part is important for conferring the immunity phenotype. A concept based on target shielding is proposed for the PepI immunity mechanism.

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35

Barba Colmenero, Vicente, Juan Antonio Martínez Hermoso, Antonio Tomás Mozas Calvache, José Luis Pérez García, and Alejandro Jiménez Serrano. "De tumba a iglesia. Análisis arqueológico y arquitectónico del complejo funerario del Reino Antiguo (QH34h) y su transformación en iglesia cristiana bizantina en la necrópolis de Qubbet el Hawa (Asuán, Egipto)." Arqueología de la Arquitectura, no. 19 (April 6, 2022): e126. http://dx.doi.org/10.3989/arq.arqt.2022.003.

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El yacimiento arqueológico de Qubbet el-Hawa alberga una de las mayores necrópolis del sur de Egipto. En ella se enterraron los altos dignatarios y los nobles que gobernaron la provincia más meridional de Egipto desde el Reino Antiguo (al menos la VI dinastía) hasta el Reino Medio (Dinastía XII). Se han llegado a documentar más de 70 hipogeos, alguno de los cuales aún siguen sin ser investigados en profundidad. El trabajo que aquí presentamos trata de comprender uno de los complejos funerarios más grandes y antiguos de la necrópolis, compuesto por la tumba conocida como QH34h, que perteneció al gobernador Khunes y las tumbas anexas de sus familiares. Fue construido hacia el final del reinado de Pepy II (2216-2153 a. C.), sufrió una serie de transformaciones arquitectónicas a lo largo de su historia, derrumbes importantes y finalmente fue elegido por una comunidad monástica para establecer en él una iglesia cristiana en el siglo VI. El objetivo principal de este artículo es analizar cómo un espacio sagrado cambió a lo largo del tiempo y los diferentes espacios arquitectónicos fueron usados en diferentes propósitos.

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36

Dardevet, D., M. C. Moore, D. Neal, C. A. DiCostanzo, W. Snead, and A. D. Cherrington. "Insulin-independent effects of GLP-1 on canine liver glucose metabolism: duration of infusion and involvement of hepatoportal region." American Journal of Physiology-Endocrinology and Metabolism 287, no. 1 (July 2004): E75—E81. http://dx.doi.org/10.1152/ajpendo.00035.2004.

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Whether glucagon-like peptide-1 (GLP-1) has insulin-independent effects on glucose disposal in vivo was assessed in conscious dogs by use of tracer and arteriovenous difference techniques. After a basal period, each experiment consisted of three periods (P1, P2, P3) during which somatostatin, glucagon, insulin, and glucose were infused. The control group (C) received saline in P1, P2, and P3, the PePe group received saline in P1 and GLP-1 (7.5 pmol·kg−1·min−1) peripherally (Pe; iv) in P2 and P3, and the PePo group received saline in P1 and GLP-1 peripherally (iv) (P2) and then into the portal vein (Po; P3). Glucose and insulin concentrations increased to two- and fourfold basal, respectively, and glucagon remained basal. GLP-1 levels increased similarly in the PePe and PePo groups during P2 (∼200 pM), whereas portal GLP-1 levels were significantly increased (3-fold) in PePo vs. PePe during P3. In all groups, net hepatic glucose uptake (NHGU) occurred during P1. During P2, NHGU increased slightly but not significantly in all groups. During P3, NHGU increased in PePe and PePo groups to a greater extent than in C, but no significant effect of the route of infusion of GLP-1 was demonstrated (16.61 ± 2.91 and 14.67 ± 2.09 vs. 4.22 ± 1.57 μmol·kg−1·min−1, respectively). In conclusion: GLP-1 increased glucose disposal in the liver independently of insulin secretion; its full action required long-term infusion. The route of infusion did not modify the hepatic response.

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Finnegan, Loretta P., Jacques Rossouw, and William R. Harlan. "A peppy response to PEPI results." Nature Medicine 1, no. 3 (March 1995): 205–6. http://dx.doi.org/10.1038/nm0395-205.

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38

MacGregor, Graham, and T. Antonios. "Pep(pery) talk on salt." Lancet 348, no. 9039 (November 1996): 1453. http://dx.doi.org/10.1016/s0140-6736(04)70099-9.

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39

Kesumawati, E., Sabaruddin, E. Hayati, N. Hadisah, R. Hayati, Y. Haidar, N. S. Pohan, et al. "Genetic variance and heritability estimation of hybridized pepper plants (Capsicum annuum L.) F2 progeny for begomovirus resistance in growth stage." IOP Conference Series: Earth and Environmental Science 951, no. 1 (January 1, 2022): 012103. http://dx.doi.org/10.1088/1755-1315/951/1/012103.

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Abstract Pepper is widely cultivated as a condiment and cash crop in Indonesia. However, Pepper yellow leaf curl disease (PepYLCD) caused by begomovirus is currently seriously affect the domestic pepper production. Breeding for begomovirus resistance material by crossing is currently necessary to overcome the constraint. The present study is aimed to determine the resistance of pepper (C. annuum) plants F2 progenies to begomovirus infection in the growth stage. Two local C. annuum accessions, BaPep-5 as a resistance donor for pepy-1 begomovirus resistance gene (locally called Perintis) and BaPep-4 as a susceptible parent (locally called Kencana) were crossed to generate F2 progenies. The research was conducted in Agricultural Extension Training Centre (BLPP) Saree and Horticulture Laboratory of Syiah Kuala University from February to July 2020. 500 F2 progenies were transplanted to the field along with 15 plants of each parent as control. The result suggested that plant height and crown width had the highest broad sense heritability value, whereas the dichotomous height, stem diameter, secondary branch, and tertiary branch had the lowest broad sense heritability value. Coefficient of genetic variance and coefficient of phenotypic variance from overall characteristics were relatively low which suggest the narrow sense to slightly narrow sense heritability.

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Meyer, Claudia, Gabriele Bierbaum, Christoph Heidrich, Michaela Reis, Jorg Suling, Maria I. Iglesias-Wind, Christoph Kempter, Ernst Molitor, and Hans-Georg Sahl. "Nucleotide Sequence of the Lantibiotic Pep5 Biosynthetic Gene Cluster and Functional Analysis of PepP and PepC. Evidence for a Role of PepC in Thioether Formation." European Journal of Biochemistry 232, no. 2 (September 1995): 478–89. http://dx.doi.org/10.1111/j.1432-1033.1995.tb20834.x.

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&NA;. "PEPI peps up the heat on HRT." Inpharma Weekly &NA;, no. 971 (January 1995): 5. http://dx.doi.org/10.2165/00128413-199509710-00007.

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42

He, Xiaojuan, Qin Li, Nan Wang, and Sanfeng Chen. "Effects of an EPS Biosynthesis Gene Cluster of Paenibacillus polymyxa WLY78 on Biofilm Formation and Nitrogen Fixation under Aerobic Conditions." Microorganisms 9, no. 2 (January 30, 2021): 289. http://dx.doi.org/10.3390/microorganisms9020289.

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Exopolysaccharides (EPS) are of high significance in bacterial biofilm formation. However, the effects of EPS cluster(s) on biofilm formation in Paenibacillus species are little known. In this study, we have shown that Paenibacillus polymyxa WLY78, a N2-fixing bacterium, can form biofilm. EPS is the major component of the extracellular matrix. The genome of P. polymyxa WLY78 contains two putative gene clusters (designated pep-1 cluster and pep-2 cluster). The pep-1 cluster is composed of 12 putative genes (pepO-lytR) co-located in a 13 kb region. The pep-2 cluster contains 17 putative genes (pepA-pepN) organized as an operon in a 20 kb region. Mutation analysis reveals that the pep-2 cluster is involved in EPS biosynthesis and biofilm formation. Disruption of the pep-2 cluster also leads to the enhancement of motility and change of the colony morphology. In contrast, disruption of the pep-1 cluster does not affect EPS synthesis or biofilm formation. More importantly, the biofilm allowed P. polymyxa WLY78 to fix nitrogen in aerobic conditions, suggesting that biofilm may provide a microaerobic environment for nitrogenase synthesis and activity.

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den Hengst, Chris D., Peter Curley, Rasmus Larsen, Girbe Buist, Arjen Nauta, Douwe van Sinderen, Oscar P. Kuipers, and Jan Kok. "Probing Direct Interactions between CodY and the oppD Promoter of Lactococcus lactis." Journal of Bacteriology 187, no. 2 (January 15, 2005): 512–21. http://dx.doi.org/10.1128/jb.187.2.512-521.2005.

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ABSTRACT CodY of Lactococcus lactis MG1363 is a transcriptional regulator that represses the expression of several genes encoding proteins of the proteolytic system. These genes include pepN, pepC, opp-pepO1, and probably prtPM, pepX, and pepDA2, since the expression of the latter three genes relative to nitrogen availability is similar to that of the former. By means of in vitro DNA binding assays and DNase I footprinting techniques, we demonstrate that L. lactis CodY interacts directly with a region upstream of the promoter of its major target known so far, the opp system. Our results indicate that multiple molecules of CodY interact with this promoter and that the amount of bound CodY molecules is affected by the presence of branched-chain amino acids and not by GTP. Addition of these amino acids strongly affects the extent of the region protected by CodY in DNase I footprints. Random and site-directed mutagenesis of the upstream region of oppD yielded variants that were derepressed in a medium with an excess of nitrogen sources. Binding studies revealed the importance of specific bases in the promoter region required for recognition by CodY.

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Dardevet, Dominique, Mary Courtney Moore, Catherine A. DiCostanzo, Ben Farmer, Doss W. Neal, Wanda Snead, Margaret Lautz, and Alan D. Cherrington. "Insulin secretion-independent effects of GLP-1 on canine liver glucose metabolism do not involve portal vein GLP-1 receptors." American Journal of Physiology-Gastrointestinal and Liver Physiology 289, no. 5 (November 2005): G806—G814. http://dx.doi.org/10.1152/ajpgi.00121.2005.

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Whether glucagon-like peptide (GLP)-1 requires the hepatic portal vein to elicit its insulin secretion-independent effects on glucose disposal in vivo was assessed in conscious dogs using tracer and arteriovenous difference techniques. In study 1, six conscious overnight-fasted dogs underwent oral glucose tolerance testing (OGTT) to determine target GLP-1 concentrations during clamp studies. Peak arterial and portal values during OGTT ranged from 23 to 65 pM and from 46 to 113 pM, respectively. In study 2, we conducted hyperinsulinemic-hyperglycemic clamp experiments consisting of three periods (P1, P2, and P3) during which somatostatin, glucagon, insulin and glucose were infused. The control group received saline, the PePe group received GLP-1 (1 pmol·kg−1·min−1) peripherally, the PePo group received GLP-1 (1 pmol·kg−1·min−1) peripherally (P2) and then intraportally (P3), and the PeHa group received GLP-1 (1 pmol·kg−1·min−1) peripherally (P2) and then through the hepatic artery (P3) to increase the hepatic GLP-1 load to the same extent as in P3 in the PePo group ( n = 8 dogs/group). Arterial GLP-1 levels increased similarly in all groups during P2 (∼50 pM), whereas portal GLP-1 levels were significantly increased (2-fold) in the PePo vs. PePe and PeHa groups during P3. During P2, net hepatic glucose uptake (NHGU) increased slightly but not significantly (vs. P1) in all groups. During P3, GLP-1 increased NHGU in the PePo and PeHa groups more than in the control and PePe groups (change of 10.8 ± 1.3 and 10.6 ± 1.0 vs. 5.7 ± 1.0 and 5.4 ± 0.8 μmol·kg−1·min−1, respectively, P < 0.05). In conclusion, physiological GLP-1 levels increase glucose disposal in the liver, and this effect does not involve GLP-1 receptors located in the portal vein.

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Lu, Jun, Yong Wu, Juanli Yuan, Jin Yuan, Zhongliang Wang, Jinyan Gao, and Hongbing Chen. "Characterization of Bacillus cereus AFA01 Capable of Degrading Gluten and Celiac-Immunotoxic Peptides." Foods 10, no. 8 (July 26, 2021): 1725. http://dx.doi.org/10.3390/foods10081725.

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Wheat gluten elicits a pro-inflammatory immune response in patients with celiac disease. The only effective therapy for this disease is a life-long gluten-free diet. Gluten detoxification using glutenases is an alternative approach. A key step is to identify useful glutenases or glutenase-producing organisms. This study investigated the gluten-degrading activity of three Bacillus cereus strains using gluten, gliadin, and highly immunotoxic 33- and 13-mer gliadin peptides. The strain AFA01 was grown on four culture media for obtaining the optimum gluten degradation. Complete genome sequencing was performed to predict genes of enzymes with potential glutenase activity. The results showed that the three B. cereus strains can hydrolyze gluten, immunotoxic peptides, and gliadin even at pH 2.0. AFA01 was the most effective strain in degrading the 33-mer peptide into fractions containing less than nine amino acid residues, the minimum peptide to induce celiac responses. Moreover, growth on starch casein broth promoted AFA01 to degrade immunotoxic peptides. PepP, PepX, and PepI may be responsible for the hydrolysis of immunotoxic peptides. On the basis of the potential of gluten degradation, AFA01 or its derived enzymes may be the best option for further research regarding the elimination of gluten toxicity.

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Robert Oluwaseyi Ogede, Nurudeen Abdulafeez Abdulrahman, and Dasola Airat Apata. "DFT computational study of pyridazine derivatives as corrosion inhibitors for mild steel in acidic media." GSC Advanced Research and Reviews 11, no. 3 (June 30, 2022): 106–14. http://dx.doi.org/10.30574/gscarr.2022.11.3.0151.

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The molecular structures of two Pyridazine derivative;5-phenyl-6-ethyl-pyridazine-3-thione (PEPT) and 5-phenyl-6-ethylpridazine-3-one (PEPO) were simulated for corrosion inhibition efficiency using quantum chemical calculations based on density functional theory (DFT) at the B3LYP/6-31G* basis set level in order to compare the relationship between their molecular structure,electronic structure and inhibition potential.The quantum chemical properties for inhibition efficiency such as EHOMO (energy of the highest occupied molecular orbital), ELUMO (energy of the lowest unoccupied molecular orbital), energy gap (ΔE), dipole moment (μ), global hardness (η), global softness (S), electronegativity (χ), electrophilicity (ω), nucleophilicity (ɛ), electrons transferred from inhibitors to metal surface (ΔN), and the energy change during electronic back-donation process (ΔE*) were calculated. The results show that 5-phenyl-6-ethyl-pyridazine-3-thione (PEPT) would have higher inhibition efficiency than 5-phenyl-6-ethylpridazine-3-one (PEPO) due to its relative EHOMO, ELUMO, ΔE, μ, η, S , ꭓ, ω, ΔN, and ∆E*.

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Neu, T., and B. Henrich. "New Thermosensitive Delivery Vector and Its Use To Enable Nisin-Controlled Gene Expression in Lactobacillus gasseri." Applied and Environmental Microbiology 69, no. 3 (March 2003): 1377–82. http://dx.doi.org/10.1128/aem.69.3.1377-1382.2003.

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ABSTRACT Derivatives of a cryptic plasmid from Lactobacillus curvatus showed temperature-sensitive replication in thermophilic lactobacilli. The thermosensitive replicon was used to construct the new delivery vector pTN1, which allows site-specific replacement of chromosomal DNA sequences. pTN1 carries an erythromycin resistance marker suitable for selection of single-copy integrants and replicates readily at 35°C, whereas replication is efficiently shut down at 42°C. To demonstrate the functionality of pTN1, the signal transduction genes (nisRK) of the nisin-controlled expression system were integrated downstream of the pepN gene into the chromosome of Lactobacillus gasseri. In the resulting strain, UKLbg1, expression of nisRK was likely driven by cotranscription with pepN and enabled nisin-dependent induction of a fusion of a reporter gene (pepI) to the nisA promoter. The induction rates were correlated with the amount of nisin used, and maximum pepI expression was achieved with nisin concentrations (above 25 ng/ml) at which growth of the bacteria was already inhibited.

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Shen, Nuo, Yanping Jing, Guoqing Tu, Aigen Fu, and Wenzhi Lan. "Danger-Associated Peptide Regulates Root Growth by Promoting Protons Extrusion in an AHA2-Dependent Manner in Arabidopsis." International Journal of Molecular Sciences 21, no. 21 (October 27, 2020): 7963. http://dx.doi.org/10.3390/ijms21217963.

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Plant elicitor peptides (Peps) are damage/danger-associated molecular patterns (DAMPs) that are derived from precursor proteins PROPEPs and perceived by a pair of leucine-rich repeat receptor-like kinases (LRR-RLKs), PEPR1 and PEPR2, to enhance innate immunity and to inhibit root growth in Arabidopsis thaliana. In this study, we show that Arabidopsis Pep1 inhibits the root growth by interfering with pH signaling, as acidic condition increased, but neutral and alkaline conditions decreased the Pep1 effect on inhibiting the root growth. The perception of Pep1 to PEPRs activated the plasma membrane-localized H+-ATPases (PM H+-ATPases) —the pump proton in plant cell—to extrude the protons into apoplast, and induced an overly acidic environment in apoplastic space, which further promoted the cell swelling in root apex and inhibited root growth. Furthermore, we revealed that pump proton AUTOINHIBITED H+-ATPase 2 (AHA2) physically interacted with PEPR2 and served downstream of the Pep1-PEPRs signaling pathway to regulate Pep1-induced protons extrusion and root growth inhibition. In conclusion, this study demonstrates a previously unrecognized signaling crosstalk between Pep1 and pH signaling to regulate root growth.

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Christensen, Jeffrey E., and James L. Steele. "Impaired Growth Rates in Milk of Lactobacillus helveticus Peptidase Mutants Can Be Overcome by Use of Amino Acid Supplements." Journal of Bacteriology 185, no. 11 (June 1, 2003): 3297–306. http://dx.doi.org/10.1128/jb.185.11.3297-3306.2003.

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ABSTRACT To evaluate the contribution of intracellular peptidases to the growth of the 14-amino-acid (aa) auxotroph Lactobacillus helveticus CNRZ32, single- and multiple-peptidase-deletion mutants were constructed. Two broad-specificity aminopeptidases (PepC and PepN) and X-prolyl dipeptidyl aminopeptidase (PepX) were inactivated through successive cycles of chromosomal gene replacement mutagenesis. The inactivation of all three peptidases in JLS247 (ΔpepC ΔpepN ΔpepX) did not affect the growth rate in amino acid-defined medium. However, the peptidase mutants generally had decreased specific growth rates when acquisition of amino acids required hydrolysis of the proteins in milk, the most significant result being a 73% increase in generation time for JLS247. The growth rate deficiencies in milk were overcome by amino acid supplements with some specificity to each of the peptidase mutants. For example, milk supplementation with Pro resulted in the most significant growth rate increase for ΔpepX strains and a 7-aa supplement (Asn, Cys, Ile, Pro, Ser, Thr, and Val) resulted in a JLS247 growth rate indistinguishable from that of the wild type. Our results show that characterization of the activities of the broad-specificity aminopeptidases had little predictive value regarding the amino acid supplements found to enhance the milk growth rates of the peptidase mutant strains. These results represent the first determination of the physiological roles with respect to specific amino acid requirements for peptidase mutants grown in milk.

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Jing, Yanping, Nuo Shen, Xiaojiang Zheng, Aigen Fu, Fugeng Zhao, Wenzhi Lan, and Sheng Luan. "Danger-Associated Peptide Regulates Root Immune Responses and Root Growth by Affecting ROS Formation in Arabidopsis." International Journal of Molecular Sciences 21, no. 13 (June 28, 2020): 4590. http://dx.doi.org/10.3390/ijms21134590.

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Plant elicitor peptides (Peps) are damage/danger-associated molecular patterns (DAMPs) that are perceived by a pair of receptor-like kinases, PEPR1 and PEPR2, to enhance innate immunity and induce the growth inhibition of root in Arabidopsis thaliana. In this study, we show that PEPR1 and PEPR2 function vitally in roots to regulate the root immune responses when treating the roots with bacterial pathogen Pst DC3000. PEPR2, rather than PEPR1, played a predominant role in the perception of Pep1 in the roots and further triggered a strong ROS accumulation—the substance acts as an antimicrobial agent or as a secondary messenger in plant cells. Consistently, seedlings mutating two major ROS-generating enzyme genes, respiratory burst oxidase homologs D and F (RBOHD and RBOHF), abolished the root ROS accumulation and impaired the growth inhibition of the roots induced by Pep1. Furthermore, we revealed that botrytis-induced kinase 1 (BIK1) physically interacted with PEPRs and RBOHD/F, respectively, and served downstream of the Pep1-PEPRs signaling pathway to regulate Pep1-induced ROS production and root growth inhibition. In conclusion, this study demonstrates a previously unrecognized signaling crosstalk between Pep1 and ROS signaling to regulate root immune response and root growth.

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Journal articles on the topic 'Pepy I'

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