Journal articles: 'Pectate lyase'

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Boland, Whitney E., Emily DeCrescenzo Henriksen, and Joy Doran-Peterson. "Characterization of Two Paenibacillus amylolyticus Strain 27C64 Pectate Lyases with Activity on Highly Methylated Pectin." Applied and Environmental Microbiology 76, no. 17 (July 9, 2010): 6006–9. http://dx.doi.org/10.1128/aem.00043-10.

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ABSTRACT Two pectate lyases were identified from Paenibacillus amylolyticus 27C64; both enzymes demonstrated activity on methylated pectin in addition to polygalacturonic acid. PelA is in a subclass of the pectate lyase family III. PelB shows some features of pectate lyase family I but is highly divergent.

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Kikuchi, Taisei, Hajime Shibuya, Takuya Aikawa, and John T. Jones. "Cloning and Characterization of Pectate Lyases Expressed in the Esophageal Gland of the Pine Wood Nematode Bursaphelenchus xylophilus." Molecular Plant-Microbe Interactions® 19, no. 3 (March 2006): 280–87. http://dx.doi.org/10.1094/mpmi-19-0280.

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Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xy-lophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55°C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini and the genes are expressed solely in the esophageal gland cells of the nematode, indicating that the pectate lyases could be secreted into plant tissues to help feeding and migration in the tree. This study suggests that pectate lyases are widely distributed in plant-parasitic nematodes and play an important role in plant-nematode interactions.

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Dubey, Amit Kumar, Sangeeta Yadav, Manish Kumar, Vinay Kumar Singh, Bijaya Ketan Sarangi, and Dinesh Yadav. "In Silico Characterization of Pectate Lyase Protein Sequences from Different Source Organisms." Enzyme Research 2010 (September 19, 2010): 1–11. http://dx.doi.org/10.4061/2010/950230.

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A total of 121 protein sequences of pectate lyases were subjected to homology search, multiple sequence alignment, phylogenetic tree construction, and motif analysis. The phylogenetic tree constructed revealed different clusters based on different source organisms representing bacterial, fungal, plant, and nematode pectate lyases. The multiple accessions of bacterial, fungal, nematode, and plant pectate lyase protein sequences were placed closely revealing a sequence level similarity. The multiple sequence alignment of these pectate lyase protein sequences from different source organisms showed conserved regions at different stretches with maximum homology from amino acid residues 439–467, 715–816, and 829–910 which could be used for designing degenerate primers or probes specific for pectate lyases. The motif analysis revealed a conserved Pec_Lyase_C domain uniformly observed in all pectate lyases irrespective of variable sources suggesting its possible role in structural and enzymatic functions.

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Ward, L. J., and S. H. De Boer. "Characterization of a monoclonal antibody against active pectate lyase from Erwinia carotovora." Canadian Journal of Microbiology 35, no. 6 (June 1, 1989): 651–55. http://dx.doi.org/10.1139/m89-105.

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A monoclonal antibody (2E2) produced against pectate lyase from Erwinia carotovora ssp. carotovora reacted with a 41-and a 44-kilodalton protein on Western blots of concentrated Erwinia culture supernatants resolved by sodium dodecyl sulphate – polyaerylamide gel electrophoresis. It was unequivocally shown that monoclonal 2E2 reacted with an active form of pectate lyase by affinity purifying the antigen with the monoclonal. The affinity-purified antigen was enzymatically active and moved as a single protein band in a nonequilibrium isoelectric focusing gel. Monoclonal 2E2 reacted with the pectate lyases of a diverse range of E. carotovora ssp. carotovora, ssp. atroseptica, and ssp. betavasculorum strains, as well as with one of three strains of E. chrysanthemi. The electrophoretic mobility of the major protein (44 kilodaltons) that reacted with 2E2 was identical within a subspecies but differed among subspecies.Key words: Erwinia carotovora, pectate lyase, monoclonal antibody.

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Shevchik, Vladimir E., Guy Condemine, Janine Robert-Baudouy, and Nicole Hugouvieux-Cotte-Pattat. "The Exopolygalacturonate Lyase PelW and the Oligogalacturonate Lyase Ogl, Two Cytoplasmic Enzymes of Pectin Catabolism in Erwinia chrysanthemi 3937." Journal of Bacteriology 181, no. 13 (July 1, 1999): 3912–19. http://dx.doi.org/10.1128/jb.181.13.3912-3919.1999.

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ABSTRACT Erwinia chrysanthemi 3937 secretes into the external medium several pectinolytic enzymes, among which are eight isoenzymes of the endo-cleaving pectate lyases: PelA, PelB, PelC, PelD, and PelE (family 1); PelI (family 4); PelL (family 3); and PelZ (family 5). In addition, one exo-cleaving pectate lyase, PelX (family 3), has been found in the periplasm of E. chrysanthemi. The E. chrysanthemi 3937 gene kdgC has been shown to exhibit a high degree of similarity to the genes pelY ofYersinia pseudotuberculosis and pelB ofErwinia carotovora, which encode family 2 pectate lyases. However, no pectinolytic activity has been assigned to the KdgC protein. After verification of the corresponding nucleotide sequence, we cloned a longer DNA fragment and showed that this gene encodes a 553-amino-acid protein exhibiting an exo-cleaving pectate lyase activity. Thus, the kdgC gene was renamed pelW. PelW catalyzes the formation of unsaturated digalacturonates from polygalacturonate or short oligogalacturonates. PelW is located in the bacterial cytoplasm. In this compartment, PelW action could complete the degradation of pectic oligomers that was initiated by the extracellular or periplasmic pectinases and precede the action of the cytoplasmic oligogalacturonate lyase, Ogl. Both cytoplasmic pectinases, PelW and Ogl, seem to act in sequence during oligogalacturonate depolymerization, since oligomers longer than dimers are very poor substrates for Ogl but are good substrates for PelW. The estimated number of binding subsites for PelW is three, extending from subsite −2 to +1, while it is probably two for Ogl, extending from subsite −1 to +1. The activities of the two cytoplasmic lyases, PelW and Ogl, are dependent on the presence of divalent cations, since both enzymes are inhibited by EDTA. In contrast to the extracellular pectate lyases, Ca2+ is unable to restore the activity of PelW or Ogl, while several other cations, including Co2+, Mn2+, and Ni2+, can activate both cytoplasmic lyases.

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Guevara, M. A., P. Estévez, and M. T. González-Jaén. "Multiple forms of pectic lyases and polygalacturonase from Fusarium oxysporum f,.sp. radicis lycopersici: regulation of their synthesis by galacturonic acid." Canadian Journal of Microbiology 43, no. 3 (March 1, 1997): 245–53. http://dx.doi.org/10.1139/m97-034.

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The r2 isolate of Fusarium oxysporum f.sp. radicis-lycopersici produced several pectic enzymes that differ in substrate preference, reaction mechanism, and action pattern. We detected three forms that have lyase activity, four forms with polygalacturonase activity and one form with pectinesterase activity. Lyases had an absolute requirement for calcium and pIs of 9.20, 9.00, and 8.65. The two more alkaline forms had a weak preference for pectin, whereas the other was more active on polygalacturonate. Polygalacturonases had pIs of 9.30, 7.35, 6.85, and 6.55 and were inhibited by calcium ions. Lyases and polygalacturonases were induced by galacturonic acid and were subject to catabolite repression. Induced synthesis occurred at pHs 5.5 and 8.0 and no increase in lyase activities were promoted by alkalinization of cultures. Pectin lyase had an endo mode of action, whereas pectate lyase and polygalacturonase behaved more as exoenzymes. These results are discussed in relation to the appearance of the different pectic enzymes when the fungus is confronted with a pectic polymer.Key words: Fusarium oxysporum f.sp. radicis-lycopersici, Lycopersicon esculentum, pectate lyase, pectin lyase, polygalacturonase.

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Doyle, Elizabeth A., and Kris N. Lambert. "Cloning and Characterization of an Esophageal-Gland-Specific Pectate Lyase from the Root-Knot Nematode Meloidogyne javanica." Molecular Plant-Microbe Interactions® 15, no. 6 (June 2002): 549–56. http://dx.doi.org/10.1094/mpmi.2002.15.6.549.

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Root-knot nematodes (Meloidogyne javanica) are obligate sedentary endoparasites that must penetrate the host root to initiate their life cycle. Many enzymes are secreted by the nematode to facilitate host penetration; required enzymes may include pectate lyases and cellulases. Using differential screening, a class III pectate lyase, Mj-pel-1 (M. javanica pectate lyase 1), was cloned from a library enriched for esophageal gland genes. DNA gel blotting confirmed that the Mj-pel-1 gene was of nematode origin and a member of a small multigene family. In situ hybridization localized the expression of Mj-pel-1 to the basal cells of the esophageal glands, while immunolocalization detected the protein in the esophageal glands as well as on the exterior of the nematode, confirming that the protein is secreted. When MJ-PEL-1 was expressed in Pichia pastoris, the resulting protein was active. The pH optimum of MJ-PEL-1 was 10.0, and the enzyme was five times more active on pectate than on pectin. Like other class III pectate lyases, MJ-PEL-1 also displayed an absolute requirement for Ca2+. The root-knot nematode migrates through the middle lamella of the plant root; therefore, MJ-PEL-1 may be an important enzyme early in the infection process.

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Nasser, William, Michel Faelen, Nicole Hugouvieux-Cotte-Pattat, and Sylvie Reverchon. "Role of the Nucleoid-Associated Protein H-NS in the Synthesis of Virulence Factors in the Phytopathogenic Bacterium Erwinia chrysanthemi." Molecular Plant-Microbe Interactions® 14, no. 1 (January 2001): 10–20. http://dx.doi.org/10.1094/mpmi.2001.14.1.10.

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The ability of the enterobacterium Erwinia chrysanthemi to induce pathogenesis in plant tissue is strongly related to the massive production of plant-cell-wall-degrading enzymes (pectinases, cellulases, and proteases). Additional factors, including flagellar proteins and exopolysaccharides (EPS), also are required for the efficient colonization of plants. Production of these virulence factors, particularly pectate lyases, the main virulence determinant, is tightly regulated by environmental conditions. The possible involvement of the protein H-NS in this process was investigated. The E. chrysanthemi hns gene was cloned by complementation of an Escherichia coli hns mutation. Its nucleotide sequence contains a 405-bp open reading frame that codes for a protein with 85% identity to the E. coli H-NS protein. An E. chrysanthemi hns mutant was constructed by reverse genetics. This mutant displays a reduced growth rate and motility but an increased EPS synthesis and sensitivity toward high osmolarity. Furthermore, pectate lyase production is dramatically reduced in this mutant. The hns mutation acts on at least two conditions affecting pectate lyase synthesis: induction of pectate lyase synthesis at low temperatures (25°C) is no longer observed in the hns mutant and induction of pectate lyase production occurs in the late stationary growth phase in the hns background, instead of in the late exponential growth phase as it does in the parental strain. Moreover, the E. chrysanthemi hns mutant displays reduced virulence on plants. Taken together, these data suggest that H-NS plays a crucial role in the expression of the virulence genes and in the pathogenicity of E. chrysanthemi.

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Takeyama, Matheus Mikio, Márcia Corrêa de Carvalho, Helena Sacco Carvalho, Cristiane Rodrigues Silva, Ana Paula Trovatti Uetanabaro, Andrea Miura da Costa, Joseph A. Medeiros Evaristo, Fábio César Sousa Nogueira, Ana Elizabeth Cavalcante Fai, and Maria Gabriela Bello Koblitz. "Pectinases Secretion by Saccharomyces cerevisiae: Optimization in Solid-State Fermentation and Identification by a Shotgun Proteomics Approach." Molecules 27, no. 15 (August 5, 2022): 4981. http://dx.doi.org/10.3390/molecules27154981.

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A sequential design strategy was applied to optimize the secretion of pectinases by a Saccharomyces cerevisiae strain, from Brazilian sugarcane liquor vat, on passion fruit residue flour (PFRF), through solid-state fermentation (SSF). A factorial design was performed to determine the influence variables and two rotational central composite designs were executed. The validated experimental result was of 7.1 U mL−1 using 50% PFRF (w/w), pH 5, 30 °C for 24 h, under static SSF. Polygalacturonase, pectin methyl esterase, pectin–lyase and pectate–lyase activities were 3.5; 0.08; 3.1 and 0.8 U mL−1, respectively. Shotgun proteomics analysis of the crude extract enabled the identification of two pectin–lyases, one pectate–lyase and a glucosidase. The crude enzymatic extract maintained at least 80% of its original activity at pH values and temperatures ranging from 2 to 8 and 30 to 80 °C, respectively, over 60 min incubation. Results revealed that PFRF might be a cost-effective and eco-friendly substrate to produce pectinases. Statistical optimization led to fermentation conditions wherein pectin active proteins predominated. To the extent of our knowledge, this is the first study reporting the synthesis of pectate lyase by S. cerevisiae.

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Soriano, Margarita, Pilar Diaz, and Francisco I. Javier Pastor. "Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin." Microbiology 152, no. 3 (March 1, 2006): 617–25. http://dx.doi.org/10.1099/mic.0.28562-0.

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The gene yvpA from Bacillus subtilis was cloned and expressed in Escherichia coli. It encoded a pectate lyase of 221 amino acids that was denominated PelC. The heterologously expressed enzyme was purified by His-tag affinity chromatography and characterized. PelC depolymerized polygalacturonate and pectins of methyl esterification degree from 22 % to 89 %, exhibiting maximum activity on 22 % esterified citrus pectin. It showed an absolute Ca2+ requirement and the optimum temperature and pH were 65 °C and pH 10, respectively. The deduced amino acid sequence of PelC showed 53 % identity to pectate lyase PelA from Paenibacillus barcinonensis, which was also characterized. Similarly to PelC, purified PelA showed activity on polygalacturonate and pectins with a high degree of methyl esterification. The two enzymes cleaved pectic polymers to a mixture of oligogalacturonates, indicating an endo mode of action. Analysis of activity on trigalacturonate showed that PelC cleaved it to galacturonic acid and unsaturated digalacturonate, whereas PelA did not show activity on this substrate. PelC and PelA showed high homology to a few recently identified pectate lyases of family 3 and form with them a cluster of small-sized pectate lyases from non-pathogenic micro-organisms.

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Kramer-Haimovich, H., E. Servi, T. Katan, J. Rollins, Y. Okon, and D. Prusky. "Effect of Ammonia Production by Colletotrichum gloeosporioides on pelB Activation, Pectate Lyase Secretion, and Fruit Pathogenicity." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1034–39. http://dx.doi.org/10.1128/aem.72.2.1034-1039.2006.

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ABSTRACT The accumulation of ammonia and associated tissue alkalinization predispose avocado fruit to attack by Colletotrichum gloeosporioides. Secretion of ammonia by C. gloeosporioides in the presence of KNO3 was induced by decreasing the pH from 7.0 to 4.0. When the fungus was grown at pH 4.0 or 6.0 in the absence of a nitrogen source, ammonia did not accumulate, and neither pelB (encoding pectate lyase) transcription nor pectate lyase secretion was detected. Under these nitrogen starvation conditions, only transcriptional activation of areA, which encodes the global nitrogen regulator, was detected. pelB transcription and pectate lyase secretion were both detected when C. gloeosporioides was grown at pH 6.0 in the presence of ammonia accumulated from different nitrogen sources. The early accumulation of ammonia induced early pelB expression and pectate lyase secretion. As the external pH increased from 4.0 to 6.0, transcripts of pac1, the C. gloeosporioides pacC homolog, also could be detected. Nit mutants of C. gloeosporioides, which cannot utilize KNO3 as a nitrogen source, did not secrete ammonia, alkalinize the medium, or secrete pectate lyase. If Nit mutants were grown at pH 6.0 in the presence of glutamate, then pectate lyase secretion was induced. Infiltration of 0.1 M ammonium hydroxide at pH 10 into ripening avocado fruits enhanced the activation of quiescent infection and symptom development by C. gloeosporioides. These results suggest that ambient pH alkalinization resulting from ammonia accumulation and the availability of ammonia as a nitrogen source independently regulate pelB expression, pectate lyase secretion, and virulence of C. gloeosporioides. These data suggest that alkalinization during C. gloeosporioides infection is important for its transformation from the quiescent biotrophic stage to the necrotrophic stage of fungal colonization in the fruit host.

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Songpim, Molnapat, Pilanee Vaithanomsat, and Sawitri Chuntranuluck. "Optimization of Pectate Lyase Production from Paenibacillus polymyxa N10 using Response Surface Methodology." Open Biology Journal 3, no. 1 (January 13, 2010): 1–7. http://dx.doi.org/10.2174/18741967010030100001.

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The parameters affecting the production of pectate lyase from P. polymyxa N10 were studied using the response surface methodology agitation rate (X1, 100-300 rpm), temperature (X2, 25-45 °C) and pH (X3, 5.5-9.5). The most significant factors influencing enzyme production were temperature and pH. The second order polynomial regression model obtained was fitted and found adequate, with an R2 of 0.9600 (p < 0.001). A maximum pectate lyase activity of 84.5 U/ml was attained in 72 h of cultivation at agitation rate 200 rpm, temperature 35 °C and pH 8. Optimizations of agitation rate and aeration on pectate lyase production were also carried out in a 5-l stirred-tank bioreactor. The aeration rate was varied in the range of 0.5-2 vvm at agitation rate of 200 rpm (temperature 35°C and initial pH 8). At agitation rate of 200 rpm, the shear force was high and then decreased the pectate lyase activity due to its negative effect on the enzyme structure. A maximum pectate lyase activity of 110.42 U/ml in the bioreactor was close to that obtained from the shake flask fermentation study.

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Zhou, Cheng, Yuting Cao, Yanfen Xue, Weidong Liu, Jiansong Ju, and Yanhe Ma. "Structure of an Alkaline Pectate Lyase and Rational Engineering with Improved Thermo-Alkaline Stability for Efficient Ramie Degumming." International Journal of Molecular Sciences 24, no. 1 (December 29, 2022): 538. http://dx.doi.org/10.3390/ijms24010538.

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Alkaline pectate lyases have biotechnological applications in plant fiber processing, such as ramie degumming. Previously, we characterized an alkaline pectate lyase from Bacillus clausii S10, named BacPelA, which showed potential for enzymatic ramie degumming because of its high cleavage activity toward methylated pectins in alkaline conditions. However, BacPelA displayed poor thermo-alkaline stability. Here, we report the 1.78 Å resolution crystal structure of BacPelA in apo form. The enzyme has the characteristic right-handed β-helix fold of members of the polysaccharide lyase 1 family and shows overall structural similarity to them, but it displays some differences in the details of the secondary structure and Ca2+-binding site. On the basis of the structure, 10 sites located in flexible regions and showing high B-factor and positive ΔTm values were selected for mutation, aiming to improve the thermo-alkaline stability of the enzyme. Following site-directed saturation mutagenesis and screening, mutants A238C, R150G, and R216H showed an increase in the T5015 value at pH 10.0 of 3.0 °C, 6.5 °C, and 7.0 °C, respectively, compared with the wild-type enzyme, interestingly accompanied by a 24.5%, 46.6%, and 61.9% increase in activity. The combined mutant R150G/R216H/A238C showed an 8.5 °C increase in the T5015 value at pH 10.0, and an 86.1% increase in the specific activity at 60 °C, with approximately doubled catalytic efficiency, compared with the wild-type enzyme. Moreover, this mutant retained 86.2% activity after incubation in ramie degumming conditions (4 h, 60 °C, pH 10.0), compared with only 3.4% for wild-type BacPelA. The combined mutant increased the weight loss of ramie fibers in degumming by 30.2% compared with wild-type BacPelA. This work provides a thermo-alkaline stable, highly active pectate lyase with great potential for application in the textile industry, and also illustrates an effective strategy for rational design and improvement of pectate lyases.

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Bekri, My Ali, Jos Desair, Veerle Keijers, Paul Proost, Marjo Searle-van Leeuwen, Jos Vanderleyden, and Ann vande Broek. "Azospirillum irakense Produces a Novel Type of Pectate Lyase." Journal of Bacteriology 181, no. 8 (April 15, 1999): 2440–47. http://dx.doi.org/10.1128/jb.181.8.2440-2447.1999.

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ABSTRACT The pelA gene from the N2-fixing plant-associated bacterium Azospirillum irakense, encoding a pectate lyase, was isolated by heterologous expression inEscherichia coli. Nucleotide sequence analysis of the region containing pelA indicated an open reading frame of 1,296 bp, coding for a preprotein of 432 amino acids with a typical amino-terminal signal peptide of 24 amino acids. N-terminal amino acid sequencing confirmed the processing of the protein in E. coli at the signal peptidase cleavage site predicted by nucleotide sequence analysis. Analysis of the amino acid sequence of PelA revealed no homology to other known pectinases, indicating that PelA belongs to a new pectate lyase family. PelA macerates potato tuber tissue, has an alkaline pH optimum, and requires Ca2+ for its activity. Of several divalent cations tested, none could substitute for Ca2+. Methyl-esterified pectin (with a degree of esterification up to 93%) and polygalacturonate can be used as substrates. Characterization of the degradation products formed upon incubation with polygalacturonate indicated that PelA is an endo-pectate lyase generating unsaturated digalacturonide as the major end product. Regulation ofpelA expression was studied by means of a translationalpelA-gusA fusion. Transcription of this fusion is low under all growth conditions tested and is dependent on the growth phase. In addition, pelA expression was found to be induced by pectin. An A. irakense pelA::Tn5mutant still displayed pectate lyase activity, suggesting the presence of multiple pectate lyase genes in A. irakense.

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Elumalai, R. P., and A. Mahadevan. "Characterization of pectate lyase produced by Pseudomonas marginalis and cloning of pectate lyase genes." Physiological and Molecular Plant Pathology 46, no. 2 (February 1995): 109–19. http://dx.doi.org/10.1006/pmpp.1995.1009.

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Yuan, Ye, Xin-Yu Zhang, Yan Zhao, Han Zhang, Yi-Fa Zhou, and Juan Gao. "A Novel PL9 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression, and Its Application in Pectin Degradation." International Journal of Molecular Sciences 20, no. 12 (June 22, 2019): 3060. http://dx.doi.org/10.3390/ijms20123060.

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Pectate lyases play an important role in pectin degradation, and therefore are highly useful in the food and textile industries. Here, we report on the cloning of an alkaline pectate lyase gene (pppel9a) from Paenibacillus polymyxa KF-1. The full-length gene (1350 bp) encodes for a 449-residue protein that belongs to the polysaccharide lyase family 9 (PL9). Recombinant PpPel9a produced in Escherichia coli was purified to electrophoretic homogeneity in a single step using Ni2+-NTA affinity chromatography. The enzyme activity of PpPel9a (apparent molecular weight of 45.3 kDa) was found to be optimal at pH 10.0 and 40 °C, with substrate preference for homogalacturonan type (HG) pectins vis-à-vis rhamnogalacturonan-I (RG-I) type pectins. Using HG-type pectins as substrate, PpPel9a showed greater activity with de-esterified HGs. In addition, PpPel9a was active against water-soluble pectins isolated from different plants. Using this lyase, we degraded citrus pectin, purified fractions using Diethylaminoethyl (DEAE)-sepharose column chromatography, and characterized the main fraction MCP-0.3. High-performance gel permeation chromatography (HPGPC) analysis showed that the molecular mass of citrus pectin (~230.2 kDa) was reduced to ~24 kDa upon degradation. Ultra-performance liquid chromatography - tandem mass spectrometer (UPLC-MS) and monosaccharide composition analyses demonstrated that PpPel9a worked as an endo-pectate lyase, which acted primarily on the HG domain of citrus pectin. In vitro testing showed that the degradation product MCP-0.3 significantly promotes the growth of Lactobacillus plantarum and L. rhamnosus. In this regard, the enzyme has potential in the preparation of pharmacologically active pectin products.

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Smadja, Bruno, Xavier Latour, Sameh Trigui, Jean François Burini, Sylvie Chevalier, and Nicole Orange. "Thermodependence of growth and enzymatic activities implicated in pathogenicity of twoErwinia carotovorasubspecies (Pectobacteriumspp.)." Canadian Journal of Microbiology 50, no. 1 (January 1, 2004): 19–27. http://dx.doi.org/10.1139/w03-099.

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Erwinia carotovora subsp. atroseptica and Erwinia carotovora subsp. carotovora can cause substantial damage to economically important plant crops and stored products. The occurrence of the disease and the scale of the damage are temperature dependent. Disease development consists first of active multiplication of the bacteria in the infection area and then production of numerous extracellular enzymes. We investigated the effects of various temperatures on these two steps. We assayed the specific growth rate and the pectate lyase and protease activities for eight strains belonging to E. carotovora subsp. atroseptica and E. carotovora subsp. carotovora in vitro. The temperature effect on growth rate and on pectate lyase activity is different for the two subspecies, but protease activity appears to be similarly thermoregulated. Our results are in agreement with ecological data implicating E. carotovora subsp. atroseptica in disease when the temperature is below 20 °C. The optimal temperature for pathogenicity appears to be different from the optimal growth temperature but seems to be a compromise between this temperature and temperatures at which lytic activities are maximal.Key words: temperature, Pectobacterium atrosepticum, Pectobacterium carotovorum, growth, pectate lyases, proteases.

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Saha, Monidipta, Rajib S. Rana, Biswanath Adhikary, and Sabyasachi Mitra. "Screening of bacterial strains for pectate lyase production and detection of optimal growth conditions for enhanced enzyme activity." Journal of Applied and Natural Science 9, no. 1 (March 1, 2017): 370–74. http://dx.doi.org/10.31018/jans.v9i1.1198.

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In the present study, the pectatelyase production by fifty two bacterial strains isolated from ramie grown soils were studied and the strain RDSM01 showed maximum pectate lyase activity. According to sequence homology of Genbank, the strain RDSM01 was identified as Bacillus subtilis (Genbank Accession No. KX035109). Maximum pectate lyase activity of the strain was observed when 1.5% (v/v) inoculum was added to the growth medium and was incubated for 48 hours at 34-370C and at pH 7.0. The relative activity of the strain was 19% higher when apple pectin was used as carbon source compared to citrus pectin. Maximum enzyme production (149.1 – 153.4 IU/ml) was recorded when ammonium chloride or ammonium sulphate at 0.4% concentration was used as nitrogen source. Thus, B. subtilis strain RDSM01 possessing high pectate lyase activity may be effectively utilized for removal of gum from ramie fibre, which is primarily made of pectin and hemicellulose.

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RAO, M. Narsimha, Asha A. KEMBHAVI, and Aditi PANT. "Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae." Biochemical Journal 319, no. 1 (October 1, 1996): 159–64. http://dx.doi.org/10.1042/bj3190159.

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An extracellular pectate lyase from Fusarium moniliformae was purified to homogeneity by affinity chromatography followed by gel filtration, with a yield of 76.5%. Laser desorption MS of the enzyme gave a molecular mass of 12133.5±2.5 Da. The pectate lyase was a glycoprotein with a 5% carbohydrate content and had a pI value of 9.1. Atomic-emission spectrometry showed that Ca2+ was a part of the holoenzyme held by carboxy groups of the protein. These results support the hypothesis of a putative Ca2+ site suggested by Yodder, Keen and Jurnak [(1993) Science 260, 1503–1507] in the crystal structure of pectate lyase C of Erwinia chrysanthemi. Loss of Ca2+ was observed by treatment with EGTA or carboxy-modifying Woodward's reagent K, with subsequent loss of enzyme activity. Tryptophan fluorescence quenching showed that Ca2+ does not affect binding of substrate to enzyme. Chemical-modification and substrate-protection studies showed the presence of lysine and tryptophan at or near the active site of the pectate lyase. Chemically modified enzyme showed no major structural changes as determined by CD. Amino acid analyses of native, trinitrobenzenesulphonate (TBNS)-treated and substrate-protected TNBS-treated enzyme showed that a single essential residue of lysine is present at or near the active-site. Substrate-affinity studies showed that tryptophan could be essential for substrate binding, whereas lysine could be involved in the catalysis. Fluorescence quenching further confirmed the involvement of tryptophan in substrate binding. The reaction mechanism involving β-elimination by this enzyme is discussed.

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BROWN, Ian E., Marie H. MALLEN, Simon J. CHARNOCK, Gideon J. DAVIES, and Gary W. BLACK. "Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module." Biochemical Journal 355, no. 1 (February 26, 2001): 155–65. http://dx.doi.org/10.1042/bj3550155.

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Pectate lyase 10A (Pel10A) enzyme from Pseudomonas cellulosa is composed of 649 residues and has a molecular mass of 68.5kDa. Sequence analysis revealed that Pel10A contained a signal peptide and two serine-rich linker sequences that separate three modules. Sequence similarity was seen between the 9.2kDa N-terminal module of Pel10A and family 2a carbohydrate-binding modules (CBMs). This N-terminal module of Pel10A was shown to encode an independently functional module with affinity to crystalline cellulose. A high sequence identity of 66% was seen between the 14.2kDa central module of Pel10A and the functionally uncharacterized central modules of the xylan-degrading enzymes endoxylanase 10B, arabinofuranosidase 62C and esterase 1D, also from P. cellulosa. The 35.8kDa C-terminal module of Pel10A was shown to have 30 and 36% identities with the family 10 pectate lyases from Azospirillum irakense and an alkaliphilic strain of Bacillus sp. strain KSM-P15, respectively. This His-tagged C-terminal module of the Pel10A was shown to encode an independent catalytic module (Pel10Acm). Pel10Acm was shown to cleave pectate and pectin in an endo-fashion and to have optimal activity at pH10 and in the presence of 2mM Ca2+. Highest enzyme activity was detected at 62°C. Pel10Acm was shown to be most active against pectate (i.e. polygalacturonic acid) with progressively less activity against 31, 67 and 89% esterified citrus pectins. These data suggest that Pel10A has a preference for sequences of non-esterified galacturonic acid residues. Significantly, Pel10A and the P. cellulosa rhamnogalacturonan lyase 11A, in the accompanying article [McKie, Vincken, Voragen, van den Broek, Stimson and Gilbert (2001) Biochem. J. 355, 167–177], are the first CBM-containing pectinases described to date.

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Kaewnum, S., S. Prathuangwong, and T. J. Burr. "A Pectate Lyase Homolog, xagP, in Xanthomonas axonopodis pv. glycines Is Associated with Hypersensitive Response Induction on Tobacco." Phytopathology® 96, no. 11 (November 2006): 1230–36. http://dx.doi.org/10.1094/phyto-96-1230.

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Xanthomonas axonopodis pv. glycines is the causal agent of bacterial pustule disease of soybeans. A transposon insertional mutant (KU-P-M670) of X. axonopodis pv. glycines derived from wild-type strain KU-P-34017 lost the ability to induce the hypersensitive response (HR) on tobacco and pepper but retained its HR induction capacity on cucumber, sesame, and tomato. The mutation also resulted in loss of ability to cause a potato soft rot and express pectolytic activity at pH 6.5. An approximate 1.4-kb DNA fragment carrying the transposon insertion contained a single open reading frame that showed high homology with PSTRU-3, a pectate lyase gene in X. axonopodis pv. malvacearum. Complemented KU-P-M670 regained HR induction on tobacco and also pectolytic activity. Treatment of plants with inhibitors of eukaryotic metabolism blocked HR induction by wild-type strains and by complemented KU-P-M670. The presence of the pectate lyase homolog, which we designated xagP, in 26 X. axonopodis pv. glycines strains was highly correlated with their ability to induce an HR on tobacco. To our knowledge, this is the first study indicating a role for a functional pectate lyase in induction of a plant HR.

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22

Cheng, Lifeng, Shengwen Duan, Ke Zheng, Xiangyuan Feng, Qi Yang, Zhiyuan Liu, Zhengchu Liu, and Yuande Peng. "An alkaline pectate lyase D from Dickeya dadantii DCE-01: clone, expression, characterization, and potential application in ramie bio-degumming." Textile Research Journal 89, no. 11 (August 27, 2018): 2075–83. http://dx.doi.org/10.1177/0040517518790971.

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Pectinase plays a crucial role in ramie bio-degumming. A pectate lyase gene ( pel4J4) from the high-efficiency degumming bacteria Dickeya dadantii DCE-01 of bast fibers was cloned and connected to pET28a, and then the recombinant plasmid was successfully transformed into Escherichia coli BL21(DE3). The pectate lyase (Pel4J4) induced was purified by ultrafiltration and Sephadex G-100 gel chromatography. The enzymatic properties of Pel4J4 were studied in detail. pel4J4 (GenBank accession number: KC900167) had a sequence length of 1179 bp, encoding 392 amino acids. The extracellular pectate lyase activity of pET28a- pel-BL was up to 204.4 IU/mL. The optimal temperature and pH of the purified Pel4J4 were 55℃ and 8.5, respectively. The stable temperature and pH of Pel4J4 activity were 45℃ and 8.5–10.0, respectively. The catalytic activity is Ca2+ dependent and promoted by 1 mmol/L Zn2+, Fe3+, Ca2+, and NH4+, but seriously inhibited by Cu2+ and Pb2+. The optimal substrate is citrus pectin with more than 85% esterification. The heat-resistant alkaline Pel4J4 could strongly degrade natural ramie pectin, indicating a promising application prospect in ramie bio-degumming.

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23

Bartling, S., C. Wegener, and O. Olsen. "Synergism between Erwinia pectate lyase isoenzymes that depolymerize both pectate and pectin." Microbiology 141, no. 4 (April 1, 1995): 873–81. http://dx.doi.org/10.1099/13500872-141-4-873.

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TEMSAH, M., Y. BERTHEAU, and B. VIAN. "Pectate-lyase fixation and pectate disorganization visualized by immunocytochemistry in infected by." Cell Biology International Reports 15, no. 7 (July 1991): 611–20. http://dx.doi.org/10.1016/0309-1651(91)90008-7.

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Sun, Lingxia, Sunchung Park, Martin Bukovac, and Steven van Nocker. "(98) Molecular Analysis of Abscission Layer Activation in Apple Fruit Pedicels." HortScience 41, no. 4 (July 2006): 1030B—1030. http://dx.doi.org/10.21273/hortsci.41.4.1030b.

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Abscission of leaves, floral organs, and fruit is a developmentally and environmentally regulated process initiated in specialized thin layers of cells within abscission zones (AZs). Very little is known about early molecular events that drive abscission, especially of fruit. Commercial apple production relies on the use of flower and fruit abscission-promoting and -inhibiting compounds to enhance fruit quality, control preharvest fruit drop, and maintain consistent annual bearing. The success of chemical treatments is strongly influenced by numerous factors, including environment, genotype, developmental stage of the fruit, and physiological state of the tree. Toward developing improved strategies for regulating fruit abscission, we carried out transcriptional profiling of competent-quiescent and activated abscission layers. We found that a decisive event in the sequential process of abscission layer development is the transcriptional activation of the MdPEL1 gene, encoding a plant pectate lyase protein and potentially involved in the degradation of the middle lamella of adjacent abscission layer cells. Additionally, regulatory elements of at least 12 homologous pectate lyase genes in Arabidopsis thaliana were found to direct expression in floral AZs and in dehiscence zones along valve margins, suggesting that these genes have evolutionary conserved function. This work identifies a novel role for pectate lyases in plants. Furthermore, many abscission-related genes identified in this study are being used to track biochemical and regulatory pathways that participate in abscission in response to chemical treatments or environmental effects.

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26

Smith, Drummond, and Ian Sumner. "The Stability of Bacillus Subtilis Pectate Lyase." REVIEW OF HIGH PRESSURE SCIENCE AND TECHNOLOGY 7 (1998): 1333–35. http://dx.doi.org/10.4131/jshpreview.7.1333.

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., Sathyanarayana N. Gummadi, and D. Sunil Kumar . "Pectin Lyase and Pectate Lyase from Debaryomyces nepalensis Isolated from Apple." Research Journal of Microbiology 1, no. 2 (February 1, 2006): 152–59. http://dx.doi.org/10.3923/jm.2006.152.159.

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28

Xu, Huan, Xiangyuan Feng, Qi Yang, Ke Zheng, Le Yi, Shengwen Duan, and Lifeng Cheng. "Improvement on Thermostability of Pectate Lyase and Its Potential Application to Ramie Degumming." Polymers 14, no. 14 (July 15, 2022): 2878. http://dx.doi.org/10.3390/polym14142878.

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In order to obtain a thermostable pectate lyase for ramie degumming, a rational design based on structural analysis was carried out on a novel pectate lyase (Pel419) derived from the Dickea dadantii DCE-01 for high-efficiency ramie degumming. A total of five potential amino acid sites were chosen to replace residues. Then, the mutant enzymes were subjected to the heterologous expressions in Escherichia coli and their enzymatic characteristics were determined. The optimal reaction temperature for the five mutants kept consistent with that for the wild type. The enzyme activity and thermal stability of mutant V52A were significantly improved. Meanwhile, the weight loss rate obtained by V52A with the best enzymatic characteristics in the ramie degumming process at 50 °C is comparable with that obtained by commercial cotton-ramie processing pectinases, indicating that V52A was a potential industrial enzyme that could be applied to large-scale ramie degumming. In this study, the biological functions of conservative residues of Pel419 were preliminarily explored. The mutant V52A with both enzymatic activity and improved heat resistance was acquired, providing a superior material for developing enzyme preparations of ramie degumming, and rendering an effective method for the rational design aiming to improve the thermostability of pectate lyase.

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29

Shevchik, Vladimir E., Harry C. M. Kester, Jacques A. E. Benen, Jaap Visser, Janine Robert-Baudouy, and Nicole Hugouvieux-Cotte-Pattat. "Characterization of the Exopolygalacturonate Lyase PelX of Erwinia chrysanthemi 3937." Journal of Bacteriology 181, no. 5 (March 1, 1999): 1652–63. http://dx.doi.org/10.1128/jb.181.5.1652-1663.1999.

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ABSTRACT Erwinia chrysanthemi 3937 secretes several pectinolytic enzymes, among which eight isoenzymes of pectate lyases with an endo-cleaving mode (PelA, PelB, PelC, PelD, PelE, PelI, PelL, and PelZ) have been identified. Two exo-cleaving enzymes, the exopolygalacturonate lyase, PelX, and an exo-poly-α-d-galacturonosidase, PehX, have been previously identified in other E. chrysanthemi strains. Using a genomic bank of a 3937 mutant with the major pelgenes deleted, we cloned a pectinase gene identified aspelX, encoding the exopolygalacturonate lyase. The deduced amino acid sequence of the 3937 PelX is very similar to the PelX of another E. chrysanthemi strain, EC16, except in the 43 C-terminal amino acids. PelX also has homology to the endo-pectate lyase PelL of E. chrysanthemi but has a N-terminal extension of 324 residues. The transcription of pelX, analyzed by gene fusions, is dependent on several environmental conditions. It is induced by pectic catabolic products and affected by growth phase, oxygen limitation, nitrogen starvation, and catabolite repression. Regulation of pelX expression is dependent on the KdgR repressor, which controls almost all the steps of pectin catabolism, and on the global activator of sugar catabolism, cyclic AMP receptor protein. In contrast, PecS and PecT, two repressors of the transcription of most pectate lyase genes, are not involved inpelX expression. The pelX mutant displayed reduced pathogenicity on chicory leaves, but its virulence on potato tubers or Saintpaulia ionantha plants did not appear to be affected. The purified PelX protein has no maceration activity on plant tissues. Tetragalacturonate is the best substrate of PelX, but PelX also has good activity on longer oligomers. Therefore, the estimated number of binding subsites for PelX is 4, extending from subsites −2 to +2. PelX and PehX were shown to be localized in the periplasm ofE. chrysanthemi 3937. PelX catalyzed the formation of unsaturated digalacturonates by attack from the reducing end of the substrate, while PehX released digalacturonates by attack from the nonreducing end of the substrate. Thus, the two types of exo-degrading enzymes appeared complementary in the degradation of pectic polymers, since they act on both extremities of the polymeric chain.

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30

Yakoby, Nir, Delila Beno-Moualem, Noel T. Keen, Amos Dinoor, Ophry Pines, and Dov Prusky. "Colletotrichum gloeosporioides pelB Is an Important Virulence Factor in Avocado Fruit-Fungus Interaction." Molecular Plant-Microbe Interactions® 14, no. 8 (August 2001): 988–95. http://dx.doi.org/10.1094/mpmi.2001.14.8.988.

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Colletotrichum gloeosporioides is an important pathogen of tropical and subtropical fruits. The C. gloeosporioides pelB gene was disrupted in the fungus via homologous recombination. Three independent isolates, GD-14, GD-23, and GD-29, did not produce or secrete pectate lyase B (PLB) and exhibited 25% lower pectate lyase (PL) and pectin lyase (PNL) activities and 15% higher polygalacturonase (PG) activity than the wild type. The PLB mutants exhibited no growth reduction on glucose, Na polypectate, or pectin as the sole carbon source at pH 3.8 or 6.0, except for a 15% reduction on pectin at pH 6.0. When pelB mutants were inoculated onto avocado fruits, however, a 36 to 45% reduction in estimated decay diameter was observed compared with the two controls, the wild type and undisrupted transformed isolate. In addition, these pelB mutants induced a significantly higher host phenylalanine ammonia lyase activity as well as the antifungal diene, which is indicative of higher host resistance. These results suggest that PLB is an important factor in the attack of C. gloeosporioides on avocado fruit, probably as a result of its virulence factor and role in the induction of host defense mechanisms.

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Akita, Masatake, Atsuo Suzuki, Tohru Kobayashi, Susumu Ito, and Takashi Yamane. "The first structure of pectate lyase belonging to polysaccharide lyase family 3." Acta Crystallographica Section D Biological Crystallography 57, no. 12 (November 21, 2001): 1786–92. http://dx.doi.org/10.1107/s0907444901014482.

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32

Konno, Naotake, Kiyohiko Igarashi, Naoto Habu, Masahiro Samejima, and Akira Isogai. "Cloning of the Trichoderma reesei cDNA Encoding a Glucuronan Lyase Belonging to a Novel Polysaccharide Lyase Family." Applied and Environmental Microbiology 75, no. 1 (October 31, 2008): 101–7. http://dx.doi.org/10.1128/aem.01749-08.

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ABSTRACT The filamentous fungus Trichoderma reesei produces glucuronan lyase (TrGL) when it is grown on β-(1→4)-polyglucuronate (cellouronate) as a sole carbon source. The cDNA encoding TrGL was cloned, and the recombinant enzyme was heterologously expressed in Pichia pastoris. The cDNA of TrGL includes a 777-bp open reading frame encoding a 20-amino-acid signal peptide and the 238-amino-acid mature protein. The amino acid sequence showed no similarity to the amino acid sequences of previously described functional proteins, indicating that the enzyme should be classified in a novel polysaccharide lyase (PL) family. Recombinant TrGL catalyzed depolymerization of cellouronate endolytically by β-elimination and was highly specific for cellouronate. The enzyme was most active at pH 6.5 and 50ï¿½C, and its activity and thermostability increased in the presence of Ca2+, suggesting that its calcium dependence is similar to that of other PLs, such as pectate lyases.

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33

Nasser, William, Sylvie Reverchon, Regine Vedel, and Martine Boccara. "PecS and PecT Coregulate the Synthesis of HrpN and Pectate Lyases, Two Virulence Determinants in Erwinia chrysanthemi 3937." Molecular Plant-Microbe Interactions® 18, no. 11 (November 2005): 1205–14. http://dx.doi.org/10.1094/mpmi-18-1205.

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Erwinia chrysanthemi strain 3937 is a necrotrophic bacterial plant pathogen. Pectinolytic enzymes and, in particular, pectate lyases play a key role in soft rot symptoms; however, the efficient colonization of plants by E. chrysanthemi requires additional factors. These factors include HrpN (harpin), a heat-stable, glycine-rich hydrophilic protein, which is secreted by the type III secretion system. We investigated the expression of hrpN in E. chrysanthemi 3937 in various environmental conditions and different regulatory backgrounds. Using lacZ fusions, hrpN expression was markedly influenced by the carbon source, osmolarity, growth phase, and growth substrate. hrpN was repressed when pectinolysis started and negatively regulated by the repressors of ectate lyase synthesis, PecS and PecT. Primer extension data and in vitro DNA-protein interaction experiments support a model whereby PecS represses hrpN expression by binding to the hrpN regulatory region and inhibiting transcript elongation. The results suggest coordinated regulation of HrpN and pectate lyases by PecS and PecT. A putative model of the synthesis of these two virulence factors in E. chrysanthemi during pathogenesis is presented.

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34

Dubey, Amit, Sangeeta Yadav, Manish Kumar, Gautam Anand, and Dinesh Yadav. "Molecular Biology of Microbial Pectate Lyase: A Review." British Biotechnology Journal 13, no. 1 (January 10, 2016): 1–26. http://dx.doi.org/10.9734/bbj/2016/24893.

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35

Miyairi, Kazuo, Ai Ogasawara, Akio Tonouchi, Kouzou Hosaka, Makiko Kudou, and Toshikatsu Okuno. "Low-Molecular-Weight Pectate Lyase from Streptomyces thermocarboxydus." Journal of Applied Glycoscience 51, no. 1 (2004): 1–7. http://dx.doi.org/10.5458/jag.51.1.

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36

Miyazaki, Yoshimitsu. "Purification and Characterization ofEndo-Pectate Lyase fromBacillus macerans." Agricultural and Biological Chemistry 55, no. 1 (January 1991): 25–30. http://dx.doi.org/10.1080/00021369.1991.10870530.

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37

Heikinheimo, Riikka. "Characterization of a Novel Pectate Lyase fromErwinia carotovorasubsp.carotovora." Molecular Plant-Microbe Interactions 8, no. 2 (1995): 207. http://dx.doi.org/10.1094/mpmi-8-0207.

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38

Diolez, A., F. Richaud, and A. Coleno. "Pectate lyase gene regulatory mutants of Erwinia chrysanthemi." Journal of Bacteriology 167, no. 1 (1986): 400–403. http://dx.doi.org/10.1128/jb.167.1.400-403.1986.

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39

Payasi, Anurag, and G. G. Sanwal. "Pectate lyase activity during ripening of banana fruit." Phytochemistry 63, no. 3 (June 2003): 243–48. http://dx.doi.org/10.1016/s0031-9422(03)00027-x.

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40

Novoa de Armas, H., A. Rabijns, C. Verboven, J. Desair, A. Vande Broeck, J. Vanderleyden, and C. De Ranter. "Structure of a novel pectate lyase fromAzospirillum irakense." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c110. http://dx.doi.org/10.1107/s0108767302089419.

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41

Hotchkiss, Jr, A. T., L. G. Revear, and K. B. Hicks. "Substrate depolymerization pattern ofPseudomonas viridiflavaSF-312 pectate lyase." Physiological and Molecular Plant Pathology 48, no. 1 (January 1996): 1–9. http://dx.doi.org/10.1006/pmpp.1996.0001.

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42

Denis, S., S. Terr�, Y. Bertheau, and P. Boyaval. "Factors affecting pectate lyase activity during membrane filtration." Biotechnology Techniques 4, no. 2 (1990): 127–32. http://dx.doi.org/10.1007/bf00163286.

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43

Xu, Huan, Shengwen Duan, Xiangyuan Feng, Qi Yang, Ke Zheng, Yuande Peng, and Lifeng Cheng. "Improving the Thermo-Activity and -Stability of Pectate Lyase from Dickeya dadantii DCE-01 for Ramie Degumming." Processes 9, no. 12 (November 24, 2021): 2106. http://dx.doi.org/10.3390/pr9122106.

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To improve the thermal stability of pectate lyase for ramie degumming, we modified the novel pectate lyase gene (pelG403) derived from the Dickeya dadantii DCE-01 high-efficiency ramie degumming strain by site-directed mutagenesis. Twelve mutants were acquired, wherein a prospective mutant (A129V) showed better enzyme activity and thermal stability. Compared with the wild type (PelG403), the specific enzyme activity and the optimal reaction temperature of A129V in the fermentation broth increased by 20.1%, and 5 °C, respectively. Under the conditions of 55 °C and pH 9.0, the weightlessness rate of ramie raw materials of A129V increased by 6.26%. Therefore, this study successfully improved the enzyme activity and heat resistance of PelG403 in an alkaline environment, which may contribute to the development of enzyme preparations and the elucidation of the mechanism for ramie bio-degumming.

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44

Yang, Shihui, Qiu Zhang, Jianhua Guo, Amy O. Charkowski, Bernard R. Glick, A. Mark Ibekwe, Donald A. Cooksey, and Ching-Hong Yang. "Global Effect of Indole-3-Acetic Acid Biosynthesis on Multiple Virulence Factors of Erwinia chrysanthemi 3937." Applied and Environmental Microbiology 73, no. 4 (December 22, 2006): 1079–88. http://dx.doi.org/10.1128/aem.01770-06.

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ABSTRACT Production of the plant hormone indole-3-acetic acid (IAA) is widespread among plant-associated microorganisms. The non-gall-forming phytopathogen Erwinia chrysanthemi 3937 (strain Ech3937) possesses iaaM (ASAP16562) and iaaH (ASAP16563) gene homologues. In this work, the null knockout iaaM mutant strain Ech138 was constructed. The IAA production by Ech138 was reduced in M9 minimal medium supplemented with l-tryptophan. Compared with wild-type Ech3937, Ech138 exhibited reduced ability to produce local maceration, but its multiplication in Saintpaulia ionantha was unaffected. The pectate lyase production of Ech138 was diminished. Compared with wild-type Ech3937, the expression levels of an oligogalacturonate lyase gene, ogl, and three endopectate lyase genes, pelD, pelI, and pelL, were reduced in Ech138 as determined by a green fluorescent protein-based fluorescence-activated cell sorting promoter activity assay. In addition, the transcription of type III secretion system (T3SS) genes, dspE (a putative T3SS effector) and hrpN (T3SS harpin), was found to be diminished in the iaaM mutant Ech138. Compared with Ech3937, reduced expression of hrpL (a T3SS alternative sigma factor) and gacA but increased expression of rsmA in Ech138 was also observed, suggesting that the regulation of T3SS and pectate lyase genes by IAA biosynthesis might be partially due to the posttranscriptional regulation of the Gac-Rsm regulatory pathway.

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45

Jafra, Sylwia, Izabela Figura, Nicole Hugouvieux-Cotte-Pattat, and Ewa Lojkowska. "Expression of Erwinia chrysanthemi Pectinase Genes pelI, pelL, and pelZ During Infection of Potato Tubers." Molecular Plant-Microbe Interactions® 12, no. 10 (October 1999): 845–51. http://dx.doi.org/10.1094/mpmi.1999.12.10.845.

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Erwinia chrysanthemi mutants, containing transcriptional fusions of one of the minor pectate lyase genes (pelI, pelL, pelZ) with the reporter gene encoding β-glucuronidase activity, were studied for their ability to cause disease symptoms and to synthesize pectinases after inoculation of potato tubers. The strains affected in pelI and pelL genes displayed reduced virulence on potato tubers, demonstrating the important role of these isoenzymes in soft rot disease. Inactivation of the pelZ gene slightly influences the ability to macerate. Analysis of the bacterial population showed rapid multiplication of bacteria during infection. Similar kinetics of growth were observed for all mutants and for the wild-type strain. Comparison of the mutants and the wild-type strain showed that the pelI, pelL, and pelZ mutants synthesized reduced levels of Pels. The expression of pelZ is fivefold higher in planta than in bacterial cultures. In contrast, both pelI and pelL are highly (10-fold factor) induced in planta, which is characteristic of the plant-inducible pectate lyases.

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46

Zhao, Yan, Ye Yuan, Xinyu Zhang, Yumei Li, Qiang Li, Yifa Zhou, and Juan Gao. "Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression and Characterization." Molecules 23, no. 11 (October 26, 2018): 2774. http://dx.doi.org/10.3390/molecules23112774.

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Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of Paenibacillus polymyxa KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from P. polymyxa KF-1 genomic DNA and expressed in Escherichia coli. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and pI of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The Km, vmax and kcat values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s−1, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (Boehmeria nivea) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.

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47

Yamazaki, Akihiro, Jin Li, William C. Hutchins, Lixia Wang, Jincai Ma, A. Mark Ibekwe, and Ching-Hong Yang. "Commensal Effect of Pectate Lyases Secreted fromDickeya dadantiion Proliferation ofEscherichia coliO157:H7 EDL933 on Lettuce Leaves." Applied and Environmental Microbiology 77, no. 1 (November 12, 2010): 156–62. http://dx.doi.org/10.1128/aem.01079-10.

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ABSTRACTThe outbreaks caused by enterohemorrhagicEscherichia coliO157:H7 on leafy greens have raised serious and immediate food safety concerns. It has been suggested that several phytopathogens aid in the persistence and proliferation of the human enteropathogens in the phyllosphere. In this work, we examined the influence of virulence mechanisms ofDickeya dadantii3937, a broad-host-range phytopathogen, on the proliferation of the human pathogenE. coliO157:H7 EDL933 (EDL933) on postharvest lettuce by coinoculation of EDL933 withD. dadantii3937 derivatives that have mutations in virulence-related genes. A type II secretion system (T2SS)-deficient mutant ofD. dadantii3937, A1919 (ΔoutC), lost the capability to promote the multiplication of EDL933, whereas Ech159 (ΔrpoS), a stress-responsive σ factor RpoS-deficient mutant, increased EDL933 proliferation on lettuce leaves. A spectrophotometric enzyme activity assay revealed that A1919 (ΔoutC) was completely deficient in the secretion of pectate lyases (Pels), which play a major role in plant tissue maceration. In contrast to A1919 (ΔoutC), Ech159 (ΔrpoS) showed more than 2-fold-greater Pel activity than the wild-typeD. dadantii3937. Increased expression ofpelD(encodes an endo-pectate lyase) was observed in Ech159 (ΔrpoS)in planta. These results suggest that the pectinolytic activity ofD. dadantii3937 is the dominant determinant of enhanced EDL933 proliferation on the lettuce leaves. In addition, RpoS, the general stress response σ factor involved in cell survival in suboptimal conditions, plays a role in EDL933 proliferation by controlling the production of pectate lyases inD. dadantii3937.

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48

Wagner, Christian, Olov Sterner, and Heidrun Anke. "Verticillium rexianum (SACC.) SACC., a New Producer of Monacolin K." Zeitschrift für Naturforschung C 53, no. 3-4 (April 1, 1998): 289–90. http://dx.doi.org/10.1515/znc-1998-3-421.

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Abstract From the broth of submerged cultures of Verticillium rexianum (teleomorph: Nectriopsis exigua), a mycophilic fungus growing on myxomycetes, monacolin K was isolated as a weak inhibitor of pectate lyase. Monacolin K is the first secondary metabolite described from V. rexianum.

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KLUSKENS, Leon D., Gert-Jan W. M. van ALEBEEK, Alphons G. J. VORAGEN, Willem M. de VOS, and John van der OOST. "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima." Biochemical Journal 370, no. 2 (March 1, 2003): 651–59. http://dx.doi.org/10.1042/bj20021595.

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The ability of the hyperthermophilic bacterium Thermotoga maritima to grow on pectin as a sole carbon source coincides with the secretion of a pectate lyase A (PelA) in the extracellular medium. The pelA gene of T. maritima was functionally expressed in Escherichia coli as the first heterologously produced thermophilic pectinase, and purified to homogeneity. Gel filtration indicated that the native form of PelA is tetrameric. Highest activity (422units/mg, with a Km of 0.06mM) was demonstrated on polygalacturonic acid (PGA), whereas pectins with an increasing degree of methylation were degraded at a decreasing rate. In the tradition of pectate lyases, PelA demonstrated full dependency on Ca2+ for stability and activity. The enzyme is highly thermoactive and thermostable, operating optimally at 90°C and pH9.0, with a half-life for thermal inactivation of almost 2h at 95°C, and an apparent melting temperature of 102.5°C. Detailed characterization of the product formation with PGA indicated that PelA has a unique eliminative exo-cleavage pattern liberating unsaturated trigalacturonate as the major product, in contrast with unsaturated digalacturonate for other exopectate lyases known. The unique exo-acting mode of action was supported by progression profiles of PelA on oligogalacturonides (degree of polymerization, 3—8) and the examination of the bond cleavage frequencies.

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Barre, Annick, Hélène Sénéchal, Christophe Nguyen, Claude Granier, Pierre Rougé, and Pascal Poncet. "Identification of Potential IgE-Binding Epitopes Contributing to the Cross-Reactivity of the Major Cupressaceae Pectate-Lyase Pollen Allergens (Group 1)." Allergies 2, no. 3 (September 5, 2022): 106–18. http://dx.doi.org/10.3390/allergies2030010.

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Pectate-lyase allergens, the group 1 of allergens from Cupressaceae pollen, consist of glycoproteins exhibiting an extremely well-conserved three-dimensional structure and sequential IgE-binding epitopes. Up to 10 IgE-binding epitopic regions were identified on the molecular surface, which essentially cluster at both extremities of the long, curved β-prism-shaped allergens. Most of these IgE-binding epitopes possess very similar conformations that provide insight into the IgE-binding cross-reactivity and cross-allergenicity commonly observed among Cupressaceae pollen allergens. Some of these epitopic regions coincide with putative N-glycosylation sites that most probably consist of glycotopes or cross-reactive carbohydrate determinants, recognized by the corresponding IgE antibodies from allergic patients. Pectate-lyase allergens of Cupressaceae pollen offer a nice example of structurally conserved allergens that are widely distributed in closely-related plants (Chamæcyparis, Cryptomeria, Cupressus, Hesperocyparis, Juniperus, Thuja) and responsible for frequent cross-allergenicity.

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Journal articles on the topic 'Pectate lyase'

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