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Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family.
J Bacteriol. 1997 Dec; 179(23):7321-30.JB

Abstract

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.

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Authors+Show Affiliations

Shevchik VE
Laboratoire de Génétique Moléculaire des Microorganismes, UMR-CNRS 5577, INSA, Villeurbanne, France.
Robert-Baudouy J
No affiliation info available
Hugouvieux-Cotte-Pattat N
No affiliation info available

MeSH

Amino Acid SequenceChicoryChromosome MappingCloning, MolecularDickeya chrysanthemiErwiniaGene Expression Regulation, BacterialIsoenzymesMolecular Sequence DataPolysaccharide-LyasesRecombinant Fusion ProteinsRepressor ProteinsSequence Analysis, DNASequence Homology, Amino AcidSolanum tuberosumSpecies Specificity

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9393696

Citation

Shevchik, V E., et al. "Pectate Lyase PelI of Erwinia Chrysanthemi 3937 Belongs to a New Family." Journal of Bacteriology, vol. 179, no. 23, 1997, pp. 7321-30.
Shevchik VE, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N. Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family. J Bacteriol. 1997;179(23):7321-30.
Shevchik, V. E., Robert-Baudouy, J., & Hugouvieux-Cotte-Pattat, N. (1997). Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family. Journal of Bacteriology, 179(23), 7321-30.
Shevchik VE, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N. Pectate Lyase PelI of Erwinia Chrysanthemi 3937 Belongs to a New Family. J Bacteriol. 1997;179(23):7321-30. PubMed PMID: 9393696.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family. AU - Shevchik,V E, AU - Robert-Baudouy,J, AU - Hugouvieux-Cotte-Pattat,N, PY - 1997/12/11/pubmed PY - 1997/12/11/medline PY - 1997/12/11/entrez SP - 7321 EP - 30 JF - Journal of bacteriology JO - J Bacteriol VL - 179 IS - 23 N2 - 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. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/9393696/Pectate_lyase_PelI_of_Erwinia_chrysanthemi_3937_belongs_to_a_new_family_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=9393696 DB - PRIME DP - Unbound Medicine ER -