Relevant bibliographies by topics / Pectate lyase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
  5. Reports

Academic literature on the topic 'Pectate lyase'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 March 2023

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Journal articles on the topic "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
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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 showe
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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 pect
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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
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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. L
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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
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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. chrysa
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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,
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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 pecta
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Dissertations / Theses on the topic "Pectate lyase"

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Allen, Caitilyn. "Evolution of a gene for pathogenicity: endo-pectate lyase." Diss., Virginia Polytechnic Institute and State University, 1987. http://hdl.handle.net/10919/82610.

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Erwinia carotovora subsp. Carotovora (Ecc) and Erwinia carotovora subsp. Atroseptica (Eca) are plant pathogenic bacteria that cause soft rot disease of many plant species and blackleg disease of potatoes, respectively. Ecc and Eca attack plants by means of a group of extracellular plant tissue-degrading enzymes. which rapidly breaks down the pectic polymers that form a structurally important part of the plant cell wall, is considered central to soft rot pathogenesis. In this work, I isolated and studied the genes encoding this enzyme from Ecc and Eca. A clone library of Ecc strain EC14 was con
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Marín-Rodríguez, María Celia. "Investigation of the role of pectate lyase in banana fruit softening." Thesis, University of Greenwich, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.399345.

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To, Teng Teng. "Structural studies of three enzymes : telomerase, the methyltransferase CobJ and pectate lyase." Thesis, Queen Mary, University of London, 2011. http://qmro.qmul.ac.uk/xmlui/handle/123456789/691.

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This thesis investigates the structure and function of three enzymes of biotechnological and biomedical interest: telomerase from Caenorhabtidis elegans, pectate lyase from Bacillus subtilis and the methyltransferase CobJ from Rhodobacter capsulatus. Telomerase is a ribonucleoprotein found in all eukaryotes and its function is to maintain telomere length, sustain chromosome integrity and circumvent the end-replication problem. The protein requires two subunits to function, telomerase reverse transcriptase (TERT), the catalytic component, and an intrinsic RNA template (TR). The TR makes telomer
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Hounsa, Charlemagne-Gilles. "Optimisation en milieu minimum de la production d'une pectate lyase de bactéroïdes clonée chez Escherichia coli." Lille 1, 1994. http://www.theses.fr/1994LIL10006.

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L'etude a porte sur l'optimisation en milieu minimum de la production d'une pectate lyase (ec 4. 2. 2. 2) de bacteroides thetaiotaomicron 217 clonee chez escherichia coli hb101 (pbt4). Cette etude nous a conduit, a partir de l'utilisation de deux types de plans d'experiences factoriels a deux niveaux inspires du modele de box-wilson (1951), a rechercher les facteurs pouvant influencer la production de l'enzyme. Nos resultats ont montre que l'extrait de caseine, le glucose et le magnesium sont les constituants du milieu les plus influants sur la production de pectate lyase. Ces deux plans ont e
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Ladjama, Ali. "Isolement, purification et caractérisation d'une endopectate lyase d'une souche de streptomyces." Paris 5, 1991. http://www.theses.fr/1991PA05P611.

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Duprey, Alexandre. "Régulation de la transcription des gènes de virulence bactériens : dynamique des complexes nucléoprotéïques." Thesis, Lyon, 2016. http://www.theses.fr/2016LYSE1201/document.

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Les bactéries sont en permanence confrontées à des changements d'environnements. La régulation transcriptionnelle joue alors un rôle majeur dans l'adaptation des bactéries. En particulier, la bactérie phytopathogène D. dadantii s'est récemment adaptée à l'hôte végétal. Elle produit en particulier des pectate lyases (Pel) qui dégradent la pectine, ciment des parois végétales, et jouent un rôle majeur dans le développement de la maladie. Les gènes pelD et pelE, malgré la forte divergence dans leur expression, sont issus d'un transfert horizontal suivi d'une duplication récente. La question de l'
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Lyall, Mandy Marie. "The biochemical and structural analysis of two pectate lyases from polysaccharide lyase families 9 and 10 and a glycoside hydrolase belonging to family 73." Thesis, Northumbria University, 2008. http://nrl.northumbria.ac.uk/7748/.

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Othman, Babul Airianah. "Diverse mechanisms of pectic polysaccharide degradation distinguished in fruit cell walls in vivo." Thesis, University of Edinburgh, 2012. http://hdl.handle.net/1842/7878.

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Cell wall loosening and degradation are important processes in major stages of plant development including fruit ripening. Three main mechanisms have been proposed to contribute towards cell wall polysaccharide degradation in vivo: enzymic hydrolysis by endopolygalacturonase (EPG), enzymic elimination by pectate lyase (PL), and non-enzymic scission by hydroxyl radicals (•OH). However, little idea as to which of these three mechanisms predominates in homogalacturonan degradation especially during fruit ripening. This study presents an attempt to discover the respective contribution of those thr
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PISSAVIN, CHRISTINE. "Étude d'un locus de la bactérie phytopathogène erwinia chrysanthemi 3937 codant une pectate lyase et une peptidyl Prolyl cis-trans iosmérase." Paris 7, 1997. http://www.theses.fr/1997PA077265.

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Erwinia chrysanthemi est une enterobacterie phytopathogene responsable de la pourriture molle de nombreux vegetaux. Son pouvoir pathogene est du essentiellement a la production de pectinases et cellulases parmi lesquelles 8 pectate lyases (pels) sont des determinants majeurs. La plupart des pels et la cellulase celz sont exportees dans le periplasme ou elles acquierent une structure repliee grace a des catalyseurs de repliement tels que les disulfure isomerases et, probablement, des peptidyl prolyl cis-trans isomerases. L'etude de la region adjacente au locus pelb-pelc, codant deux pels, nous
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Walter, Monika. "Die parallele beta-Helix der Pektat-Lyase aus Bacillus subtilis : Stabilität, Faltungsmechanismus und Faltungsmutanten." Phd thesis, Universität Potsdam, 2002. http://opus.kobv.de/ubp/volltexte/2005/147/.

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Die Pektat-Lyasen gehören zu einer Proteinfamilie, die meistens von pflanzenpathogenen Mikroorganismen sekretiert werden. Die Enzyme katalysieren den Abbau von Polygalakturonsäure, einem Hauptbestandteil in <br /> pflanzlichen Mittellamellen und Primärzellwänden. Der Abbau der alpha-1,4-verbrückten Galakturonsäurereste erfogt durch eine beta-Eliminierungsreaktion, dabei entsteht ein Produkt mit einer ungesättigten C4-C5 Bindung am nicht reduzierenden Ende, das durch spektroskopische Messungen beobachtet werden kann. Für die enzymatische Reaktion der Pektat-Lyasen ist Calcium nötig und das pH-O
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Book chapters on the topic "Pectate lyase"

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Schomburg, Dietmar, and Margit Salzmann. "Pectate lyase." In Enzyme Handbook 1, 903–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_204.

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Elumalai, Rangasamy Periannan, and Ayyamperumal Mahadevan. "Cloning and Characterization of Pectate Lyase Genes from Pseudomonas marginalis." In Developments in Plant Pathology, 370–75. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5472-7_68.

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Hugouvieux-Cotte-Pattat, N., G. Condemine, S. Reverchon, and J. Robert-Baudouy. "Regulatory Mutants Affecting the Synthesis of Pectate Lyase of Erwinia Chrysanthemi." In Plant Pathogenic Bacteria, 259. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3555-6_48.

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Schoedel, C., K. Luttrell, and A. Collmer. "Investigation of the Relatedness of Erwinia Chrysanthemi Pectate Lyase Isozymes by Genetic and Protein Analysis." In Plant Pathogenic Bacteria, 261. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3555-6_50.

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Allan Downie, J., and Fang Xie. "A Pectate Lyase Required for Plant Cell-Wall Remodeling During Infection of Legumes by Rhizobia." In Biological Nitrogen Fixation, 575–82. Hoboken, NJ, USA: John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781119053095.ch58.

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Matsumoto, H., Y. Baba, Y. Yoshitake, P. Jitareerat, K. Nomura, and S. Tsuyumu. "Comparison of Regulatory Proteins for Pectate Lyase Synthesis between Erwinia chrysanthemi and E. carotovora subsp. carotovora." In Plant Pathogenic Bacteria, 224–28. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0003-1_51.

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Atkinson, M. M., C. J. Backer, J. S. Huang, A. Collmer, and J. A. Knopp. "Activation of a Plasmalemma K+ Efflux/H+ Influx Mechanism in Tobacco by Incompatible Bacteria or Pectate Lyase." In Plant Pathogenic Bacteria, 571. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3555-6_116.

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Esteghlalian, Ali R., Martin M. Kazaoka, David F. Walsh, Ryan T. Mccann, Arne I. Solbak, Janne Kerovuo, and Geoffrey P. Hazlewood. "Application of a Thermostable Pectate Lyase in the Bioscouring of Cotton Fabrics at Laboratory and Pilot Scales." In ACS Symposium Series, 122–36. Washington, DC: American Chemical Society, 2007. http://dx.doi.org/10.1021/bk-2007-0972.ch009.

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Jafra, S., I. Figura, N. Hugouvieux-Cotte-Pattat, and E. Lojkowska. "Characterization and Role in the Pathogenesis of Potatoes of a Novel Pectate Lyase from Eriwinia Chrysanthemi 3937." In Developments in Plant Pathology, 511–14. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-009-0043-1_113.

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Thurn, K. K., and A. K. Chatterjee. "PEL-C is the Major Pectate Lyase Produced by Erwinia Chrysanthemi (EC16) in Vitro and in Plant Tissue." In Plant Pathogenic Bacteria, 257. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3555-6_46.

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Conference papers on the topic "Pectate lyase"

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Pala, Franco, Weidong Li, and Christie Dame. "Determination of Pectate Lyase Activity in Laundry Detergents." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.256.

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Xiao, Jing, Fu-Ping Lu, Yu Li, and Jun-Xun Li. "An Unusual Pectate Lyase with Noticeable Effects on the Chinese Medicinal Herb Extract: Cloning and Characterization." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5516496.

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Reports on the topic "Pectate lyase"

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Prusky, Dov, Noel T. Keen, and Stanley Freeman. Elicitation of Preformed Antifungal Compounds by Non-Pathogenic Fungus Mutants and their Use for the Prevention of Postharvest Decay in Avocado Fruits. United States Department of Agriculture, January 1996. http://dx.doi.org/10.32747/1996.7570573.bard.

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C. gloeosporioides attacks unripe avocado fruits in the orchard. Germinated spores produce appressoria that germinate and breach the cuticle, but the resultant subcuticular hyphae become quiescent and do not develop further until fruit is harvested and ripens. Resistance of unripe avocado to attach by C. gloeosporioides is correlated with the presence of fungitoxic concentrations of the preformed antifungal compound, 1-acetoxy-2-hydroxy-4-oxoheneicosa-12, 15 diene in the pericarp of unripe fruits. The objective of this proposal was to study the signal transduction process by which elicitors in
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Prusky, Dov, and Jeffrey Rollins. Modulation of pathogenicity of postharvest pathogens by environmental pH. United States Department of Agriculture, December 2006. http://dx.doi.org/10.32747/2006.7587237.bard.

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Until recently, environmental pH was not considered a factor in determining pathogen compatibility. Our hypothesis was that the environmental pH at the infection site, which is dynamically controlled by activities of both the host and the pathogen, regulates the expression of genes necessary for disease development in Colletotrichum gloeosporioides and Sclerotinia sclerotiorum. This form of regulation ensures that genes are expressed at optimal conditions for their encoded activities.Pectate lyase encoded by pelB, has been demonstrated to play a key role in virulence of C. gloeosporioides in a
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Prusky, Dov, Lisa Vaillancourt, and Robert Fluhr. Host Ammonification by Postharvest Pathogens and its Contribution to Fungal Colonization and Symptom Development. United States Department of Agriculture, December 2006. http://dx.doi.org/10.32747/2006.7592640.bard.

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Postharvest decay of fruits and vegetables caused by pathogenic and saprophytic fungi significantly impairs the quality and quantity of fresh produce brought to market. Consequently, there is considerable interest in identifying factors that determine the susceptibility of these commodities to pathogen infection. Insidious postharvest decays remain quiescent during fruit growth and harvest, but activate during the postharvest period. A key response to the physiological changes occurring during fruit ripening is the initiation of ammonium secretion by the pathogen. Ammonium ions at the infectio
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Manulis, Shulamit, Christine D. Smart, Isaac Barash, Guido Sessa, and Harvey C. Hoch. Molecular Interactions of Clavibacter michiganensis subsp. michiganensis with Tomato. United States Department of Agriculture, January 2011. http://dx.doi.org/10.32747/2011.7697113.bard.

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Clavibacter michiganensis subsp. michiganensis (Cmm), the causal agent of bacterial wilt and canker of tomato, is the most destructive bacterial disease of tomato causing substantial economic losses in Israel, the U.S.A. and worldwide. The molecular strategies that allow Cmm, a Gram-positive bacterium, to develop a successful infection in tomato plants are largely unknown. The goal of the project was to elucidate the molecular interactions between Cmmand tomato. The first objective was to analyze gene expression profiles of susceptible tomato plants infected with pathogenic and endophytic Cmms
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