This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Shevchik, V. E. Articles by Hugouvieux-Cotte-Pattat, N. Search for Related Content PubMed PubMed Citation Articles by Shevchik, V. E. Articles by Hugouvieux-Cotte-Pattat, N.

 Previous Article  |  Next Article 

J. Bacteriol., 12 1997, 7321-7330, Vol 179, No. 23
Copyright © 1997, American Society for Microbiology

Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family

VE Shevchik, J Robert-Baudouy and N Hugouvieux-Cotte-Pattat
Laboratoire de Genetique Moleculaire des Microorganismes, UMR-CNRS 5577, INSA, Villeurbanne, France.

Erwinia chrysanthemi 3937 secretes five major isoenzymes of pectate lyases encoded by the pel4, pelB, pelC, pelD, and pelE genes and a set of secondary pectate lyases, two of which, pelL and pelZ, have been already identified. We cloned the pelI gene, encoding a ninth pectate lyase of E. chrysanthemi 3937. The pelI reading frame is 1,035 bases long, corresponding to a protein of 344 amino acids including a typical amino-terminal signal sequence of 19 amino acids. The purified mature PelI protein has an isoelectric point of about 9 and an apparent molecular mass of 34 kDa. PelI has a preference for partially methyl esterified pectin and presents an endo-cleaving activity with an alkaline pH optimum and an absolute requirement for Ca2+ ions. PelI is an extracellular protein secreted by the Out secretory pathway of E. chrysanthemi. The PelI protein is very active in the maceration of plant tissues. A pelI mutant displayed reduced pathogenicity on chicory leaves, but its virulence did not appear to be affected on potato tubers or Saintpaulia ionantha plants. The pelI gene constitutes an independent transcriptional unit. As shown for the other pel genes, the transcription of pelI is dependent on various environmental conditions. It is induced by pectic catabolic products and affected by growth phase, oxygen limitation, temperature, nitrogen starvation, and catabolite repression. Regulation of pelI expression appeared to be dependent on the three repressors of pectinase synthesis, KdgR, PecS, and PecT, and on the global activator of sugar catabolism, cyclic AMP receptor protein. A functional KdgR binding site was identified close to the putative pelI promoter. Analysis of the amino acid sequence of PelI revealed high homology with a pectate lyase from Erwinia carotovora subsp. carotovora (65% identity) and low homology with pectate lyases of the phytopathogenic fungus Nectria haematococca (Fusarium solani). This finding indicates that PelI belongs to pectate lyase class III. Using immunoblotting experiments, we detected PelI homologs in various strains of E. chrysanthemi and E. carotovora subsp. carotovora but not in E. carotovora subsp. atroseptica.

This article has been cited by other articles:

• Soriano, M., Diaz, P., Pastor, F. I. J. (2006). Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin.. Microbiology 152: 617-625 [Abstract] [Full Text]  
• Brencic, A., Winans, S. C. (2005). Detection of and Response to Signals Involved in Host-Microbe Interactions by Plant-Associated Bacteria. Microbiol. Mol. Biol. Rev. 69: 155-194 [Abstract] [Full Text]  
• Shevchik, V. E., Hugouvieux-Cotte-Pattat, N. (2003). PaeX, a Second Pectin Acetylesterase of Erwinia chrysanthemi 3937. J. Bacteriol. 185: 3091-3100 [Abstract] [Full Text]  
• Hugouvieux-Cotte-Pattat, N., Shevchik, V. E., Nasser, W. (2002). PehN, a Polygalacturonase Homologue with a Low Hydrolase Activity, Is Coregulated with the Other Erwinia chrysanthemi Polygalacturonases. J. Bacteriol. 184: 2664-2673 [Abstract] [Full Text]  
• Enard, C., Expert, D. (2000). Characterization of a tonB mutation in Erwinia chrysanthemi 3937: TonBEch is a member of the enterobacterial TonB family. Microbiology 146: 2051-2058 [Abstract] [Full Text]  
• Soriano, M., Blanco, A., Díaz, P., Pastor, F. I. J. (2000). An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization. Microbiology 146: 89-95 [Abstract] [Full Text]  
• Shevchik, V. E., Condemine, G., Robert-Baudouy, J., Hugouvieux-Cotte-Pattat, N. (1999). The Exopolygalacturonate Lyase PelW and the Oligogalacturonate Lyase Ogl, Two Cytoplasmic Enzymes of Pectin Catabolism in Erwinia chrysanthemi 3937. J. Bacteriol. 181: 3912-3919 [Abstract] [Full Text]  
• Roy, C., Kester, H., Visser, J., Shevchik, V., Hugouvieux-Cotte-Pattat, N., Robert-Baudouy, J., Benen, J. (1999). Modes of Action of Five Different Endopectate Lyases from Erwinia chrysanthemi 3937. J. Bacteriol. 181: 3705-3709 [Abstract] [Full Text]  
• Bekri, M. A., Desair, J., Keijers, V., Proost, P., Searle-van Leeuwen, M., Vanderleyden, J., vande Broek, A. (1999). Azospirillum irakense Produces a Novel Type of Pectate Lyase. J. Bacteriol. 181: 2440-2447 [Abstract] [Full Text]  
• Shevchik, V. E., Kester, H. C. M., Benen, J. A. E., Visser, J., Robert-Baudouy, J., Hugouvieux-Cotte-Pattat, N. (1999). Characterization of the Exopolygalacturonate Lyase PelX of Erwinia chrysanthemi 3937. J. Bacteriol. 181: 1652-1663 [Abstract] [Full Text]  
• Kim, J. F., Beer, S. V. (1998). HrpW of Erwinia amylovora, a New Harpin That Contains a Domain Homologous to Pectate Lyases of a Distinct Class. J. Bacteriol. 180: 5203-5210 [Abstract] [Full Text]  
• Charkowski, A. O., Alfano, J. R., Preston, G., Yuan, J., He, S. Y., Collmer, A. (1998). The Pseudomonas syringae pv. tomato HrpW Protein Has Domains Similar to Harpins and Pectate Lyases and Can Elicit the Plant Hypersensitive Response and Bind to Pectate. J. Bacteriol. 180: 5211-5217 [Abstract] [Full Text]