scholarly journals Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine-rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes.

1995 ◽  
Vol 177 (15) ◽  
pp. 4553-4556 ◽  
Author(s):  
J R Alfano ◽  
J H Ham ◽  
A Collmer
Keyword(s):  
Pectate Lyase ◽  
Erwinia Chrysanthemi ◽  
Gene Encoding

scholarly journals Expression of Erwinia chrysanthemi Pectinase Genes pelI, pelL, and pelZ During Infection of Potato Tubers

1999 ◽  
Vol 12 (10) ◽  
pp. 845-851 ◽  
Author(s):  
Sylwia Jafra ◽  
Izabela Figura ◽  
Nicole Hugouvieux-Cotte-Pattat ◽  
Ewa Lojkowska
Keyword(s):  
Type Strain ◽  
Wild Type Strain ◽  
Pectate Lyase ◽  
Soft Rot ◽  
Erwinia Chrysanthemi ◽  
Potato Tubers ◽  
Wild Type ◽  
In Planta ◽  
Gene Encoding ◽  
Glucuronidase Activity

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.

Characterization of the pelL gene encoding a novel pectate lyase of Erwinia chrysanthemi 3937

1995 ◽  
Vol 16 (6) ◽  
pp. 1183-1195 ◽  
Author(s):  
Ewa Lojkowska ◽  
Celine Masclaux ◽  
Martine Boccara ◽  
Janine Robert-Baudouy ◽  
Nicole Hugouvieux-Cotte-Pattat
Keyword(s):  
Pectate Lyase ◽  
Erwinia Chrysanthemi ◽  
Gene Encoding

scholarly journals Mutations of ousA Alter the Virulence of Erwinia chrysanthemi

2005 ◽  
Vol 18 (2) ◽  
pp. 150-157 ◽  
Author(s):  
Karine Gloux ◽  
Thierry Touze ◽  
Yves Pagot ◽  
Bernard Jouan ◽  
Carlos Blanco
Keyword(s):  
Glycine Betaine ◽  
Pectate Lyase ◽  
Inhibitory Effect ◽  
Pipecolic Acid ◽  
Erwinia Chrysanthemi ◽  
Contributory Factor ◽  
Uptake System ◽  
Potato Tubers ◽  
Low Oxygen ◽  
Gene Encoding

A negative correlation was observed between the aggressiveness of several Erwinia chrysanthemi strains on potato tuber and their osmotic tolerance. The disruption of the ousA gene encoding the major osmoprotectant uptake system highly enhanced bacterial virulence on potato tubers. The ousA disruption also increased the maceration efficiency on potato tubers under anaerobic conditions. In the absence of oxygen, pectate lyase (Pel) production was significantly higher in the tissue macerated with the ousA- strain than with the wild type. Oxygen content is significantly different between infected and healthy tissues; therefore, ousA may be a contributory factor in the infection progression within the host. In minimal medium, ousA disruption enhanced Pel production and pelE expression only under micro-aerobiosis conditions. The effect on Pel was reversed by reintroduction of the ousA gene. The osmoprotectectants glycine betaine, proline betaine, and pipecolic acid are known to be taken up via OusA and to have an inhibitory effect on Pel production. However, their effects on Pel activity were not (glycine betaine) or only weakly (proline and pipecolic acid) affected by ousA disruption. Furthermore, no correlation was observed between their effects on Pel activities and their osmoprotection efficacies. The results demonstrate a relationship between E. chrysanthemi pathogenicity factors and the activity of ousA under low oxygen status. The evidence indicates that ousA and osmoprotectant effects on Pel are not linked to osmoregulation and that complex regulations exist between Pel production, ousA, and osmoprotection via compounds liberated during the plant infection.

scholarly journals The Erwinia chrysanthemi 3937 PhoQ Sensor Kinase Regulates Several Virulence Determinants

2006 ◽  
Vol 188 (8) ◽  
pp. 3088-3098 ◽  
Author(s):  
Balakrishnan Venkatesh ◽  
Lavanya Babujee ◽  
Hui Liu ◽  
Pete Hedley ◽  
Takashi Fujikawa ◽  
...  
Keyword(s):  
Virulence Factors ◽  
Regulatory System ◽  
Soft Rot ◽  
Erwinia Chrysanthemi ◽  
Pcr Analysis ◽  
Sensor Kinase ◽  
Virulence Determinants ◽  
Gene Encoding ◽  
Reverse Transcription Pcr ◽  
Two Component

ABSTRACT The PhoPQ two-component system regulates virulence factors in Erwinia chrysanthemi, a pectinolytic enterobacterium that causes soft rot in several plant species. We characterized the effect of a mutation in phoQ, the gene encoding the sensor kinase PhoQ of the PhoPQ two-component regulatory system, on the global transcriptional profile of E. chrysanthemi using cDNA microarrays and further confirmed our results by quantitative reverse transcription-PCR analysis. Our results indicate that a mutation in phoQ affects transcription of at least 40 genes, even in the absence of inducing conditions. Enhanced expression of several genes involved in iron metabolism was observed in the mutant, including that of the acs operon that is involved in achromobactin biosynthesis and transport. This siderophore is required for full virulence of E. chrysanthemi, and its expression is governed by the global repressor protein Fur. Changes in gene expression were also observed for membrane transporters, stress-related genes, toxins, and transcriptional regulators. Our results indicate that the PhoPQ system governs the expression of several additional virulence factors and may also be involved in interactions with other regulatory systems.

D-Alanine-D-Alanine Ligase Gene (ddl) of Erwinia chrysanthemi Strain EC16 I. Isolation and Gene Dosage Effect on Pectate Lyase Synthesis

2002 ◽  
Vol 68 (4) ◽  
pp. 342-349
Author(s):  
Pongphen JITAREERAT ◽  
Hiroyuki MATSUMOTO ◽  
Masahiro UMEHARA ◽  
Shinji TSUYUMU
Keyword(s):  
Gene Dosage ◽  
Pectate Lyase ◽  
Dosage Effect ◽  
Erwinia Chrysanthemi ◽  
Gene Dosage Effect

Characterization and overexpression of the pem gene encoding pectin methylesterase of Erwinia chrysanthemi strain 3937

Gene ◽  
1993 ◽  
Vol 131 (1) ◽  
pp. 17-25 ◽  
Author(s):  
Franck Laurent ◽  
Alain Kotoujansky ◽  
Gilles Labesse ◽  
Yves Bertheau
Keyword(s):  
Pectin Methylesterase ◽  
Erwinia Chrysanthemi ◽  
Gene Encoding

Genetic and biochemical characterization of an exopolygalacturonase and a pectate lyase fromYersinia enterocolitica

1999 ◽  
Vol 45 (5) ◽  
pp. 396-403 ◽  
Author(s):  
Ching-Hsing Liao ◽  
Larry Revear ◽  
Arland Hotchkiss ◽  
Brett Savary
Keyword(s):  
High Performance ◽  
Biochemical Characterization ◽  
Amperometric Detection ◽  
Pectate Lyase ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Pathogen ◽  
Gene Encoding ◽  
Reading Frame ◽  
Chromatography Analysis

Yersinia enterocolitica, an invasive foodborne human pathogen, degrades polypectate by producing two depolymerizing enzymes, pectate lyase (PL) and polygalacturonase (PG). The gene encoding the PG activity, designated pehY, was located in a 3-kb genomic fragment of Y. enterocolitica ATCC 49397. The complete nucleotide sequence of this 3-kb fragment was determined and an open reading frame consisting of 1803 bp was predicted to encode a PG protein with an estimated Mrof 66 kDa and pI of 6.3. The amino acid sequence of prePG showed 59 and 43% identity to that of the exopolygalacturonase (exoPG) of Erwinia chrysanthemi and Ralstonia solanacearum, respectively. The Y. enterocolitica PG overproduced in Escherichia coli was purified to near homogeneity using perfusion cation exchange chromatography. Analysis of the PG depolymerization products by high performance anion-exchange chromatography and pulsed amperometric detection (HPAEC-PAD) revealed the exolytic nature of this enzyme. The Y. enterocolitica PL overproduced in E. coli was also partially purified and the Mrand pI were estimated to be 55 kDa and 5.2, respectively. HPAEC-PAD analysis of the PL depolymerization products indicated the endolytic nature of this enzyme. Southern hybridization analyses revealed that pehY and pel genes of Y. enterocolitica are possibly encoded in the chromosome rather than in the plasmid. Purified exopolygalacturonase (over 10 activity units) was unable to macerate plant tissues.Key words: pectinase activities, human pathogen, HPLC analysis, pehY gene.

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