Tags

Type your tag names separated by a space and hit enter

Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthemi 3937.
Mol Microbiol. 1995 Jun; 16(6):1183-95.MM

Abstract

Erwinia chrysanthemi 3937 secretes five major isoenzymes of pectate lyases encoded by the pelA, pelB, pelC, pelD and pelE genes. Recently, a new set of pectate lyases was identified in E. chrysanthemi mutants deleted of those pel genes. We cloned the pelL gene, encoding one of these secondary pectate lyases of E. chrysanthemi 3937, from a genomic bank of a strain deleted of the five major pel genes. The nucleotide sequence of the region containing the pelL gene was determined. The pelL reading frame is 1275 bases long, corresponding to a protein of 425 amino acids including a typical amino-terminal signal sequence of 25 amino acids. Comparison of the amino acid sequences of PelL and the exo-pectate lyase PelX of E. chrysanthemi EC16 revealed a low homology, limited to 220 residues of the central part of the proteins. No homology was detected with other bacterial pectinolytic enzymes. Regulation of pelL transcription was analysed using gene fusion. As shown for the other pel genes, the transcription of pelL is dependent on various environmental conditions. It is induced by pectic catabolic products and affected by growth phase, temperature, iron starvation, osmolarity, anaerobiosis, nitrogen starvation and catabolite repression. Regulation of pelL expression appeared to be independent of the KdgR repressor, which controls all the steps of pectin catabolism. In contrast, the pecS gene, which is involved in regulation of the synthesis of the major pectate lyases and of cellulase, also appeared to be involved in pelL expression. The PelL protein is able to macerate plant tissue. This enzyme has a basic isoelectric point, presents an endo-cleaving activity on polygalacturonate or partially methylated pectin, with a basic pH optimum and an absolute requirement for Ca2+. The pelL mutant displayed a reduced virulence on potato tubers and Saintpaulia ionantha plants, demonstrating the important role of this enzyme in soft-rot disease.

Links

Publisher Full Text

Authors+Show Affiliations

Lojkowska E
Department of Biotechnology, University of Gdansk, Poland.
Masclaux C
No affiliation info available
Boccara M
No affiliation info available
Robert-Baudouy J
No affiliation info available
Hugouvieux-Cotte-Pattat N
No affiliation info available

MeSH

Amino Acid SequenceCalcium ChlorideCell DivisionChromosome MappingDickeya chrysanthemiGene Expression Regulation, BacterialGlucuronidaseHydrogen-Ion ConcentrationIsoenzymesMolecular Sequence DataMutagenesisPectinsPlantsPolysaccharide-LyasesRecombinant Fusion ProteinsSequence AnalysisSequence Homology, Amino AcidTranscription, Genetic

Pub Type(s)

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

Language

eng

PubMed ID

8577252

Citation

Lojkowska, E, et al. "Characterization of the pelL Gene Encoding a Novel Pectate Lyase of Erwinia Chrysanthemi 3937." Molecular Microbiology, vol. 16, no. 6, 1995, pp. 1183-95.
Lojkowska E, Masclaux C, Boccara M, et al. Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthemi 3937. Mol Microbiol. 1995;16(6):1183-95.
Lojkowska, E., Masclaux, C., Boccara, M., Robert-Baudouy, J., & Hugouvieux-Cotte-Pattat, N. (1995). Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthemi 3937. Molecular Microbiology, 16(6), 1183-95.
Lojkowska E, et al. Characterization of the pelL Gene Encoding a Novel Pectate Lyase of Erwinia Chrysanthemi 3937. Mol Microbiol. 1995;16(6):1183-95. PubMed PMID: 8577252.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthemi 3937. AU - Lojkowska,E, AU - Masclaux,C, AU - Boccara,M, AU - Robert-Baudouy,J, AU - Hugouvieux-Cotte-Pattat,N, PY - 1995/6/1/pubmed PY - 1995/6/1/medline PY - 1995/6/1/entrez SP - 1183 EP - 95 JF - Molecular microbiology JO - Mol Microbiol VL - 16 IS - 6 N2 - Erwinia chrysanthemi 3937 secretes five major isoenzymes of pectate lyases encoded by the pelA, pelB, pelC, pelD and pelE genes. Recently, a new set of pectate lyases was identified in E. chrysanthemi mutants deleted of those pel genes. We cloned the pelL gene, encoding one of these secondary pectate lyases of E. chrysanthemi 3937, from a genomic bank of a strain deleted of the five major pel genes. The nucleotide sequence of the region containing the pelL gene was determined. The pelL reading frame is 1275 bases long, corresponding to a protein of 425 amino acids including a typical amino-terminal signal sequence of 25 amino acids. Comparison of the amino acid sequences of PelL and the exo-pectate lyase PelX of E. chrysanthemi EC16 revealed a low homology, limited to 220 residues of the central part of the proteins. No homology was detected with other bacterial pectinolytic enzymes. Regulation of pelL transcription was analysed using gene fusion. As shown for the other pel genes, the transcription of pelL is dependent on various environmental conditions. It is induced by pectic catabolic products and affected by growth phase, temperature, iron starvation, osmolarity, anaerobiosis, nitrogen starvation and catabolite repression. Regulation of pelL expression appeared to be independent of the KdgR repressor, which controls all the steps of pectin catabolism. In contrast, the pecS gene, which is involved in regulation of the synthesis of the major pectate lyases and of cellulase, also appeared to be involved in pelL expression. The PelL protein is able to macerate plant tissue. This enzyme has a basic isoelectric point, presents an endo-cleaving activity on polygalacturonate or partially methylated pectin, with a basic pH optimum and an absolute requirement for Ca2+. The pelL mutant displayed a reduced virulence on potato tubers and Saintpaulia ionantha plants, demonstrating the important role of this enzyme in soft-rot disease. SN - 0950-382X UR - https://www.unboundmedicine.com/medline/citation/8577252/Characterization_of_the_pelL_gene_encoding_a_novel_pectate_lyase_of_Erwinia_chrysanthemi_3937_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0950-382X&date=1995&volume=16&issue=6&spage=1183 DB - PRIME DP - Unbound Medicine ER -