Pectate lyase and polygalacturonate lyase activity in a Vi antigen-degrading enzyme preparation

Biochemistry ◽  
1970 ◽  
Vol 9 (4) ◽  
pp. 1017-1023 ◽  
Author(s):  
Lore A. McNicol ◽  
Edgar Eugene Baker
Keyword(s):  
Enzyme Preparation ◽  
Pectate Lyase ◽  
Degrading Enzyme ◽  
Lyase Activity ◽  
Polygalacturonate Lyase ◽  
Vi Antigen

Evidence against involvement of pectic enzymes in the invasion of root hairs by Rhizobium trifolii

1969 ◽  
Vol 15 (6) ◽  
pp. 643-645 ◽  
Author(s):  
James D. Macmillan ◽  
Roderic C. Cooke
Keyword(s):  
Root Hairs ◽  
Red Clover ◽  
Infection Process ◽  
Pectin Lyase ◽  
Rhizobium Trifolii ◽  
Leguminous Plants ◽  
Pectic Enzymes ◽  
Lyase Activity ◽  
Rhizobium Spp ◽  
Polygalacturonate Lyase

It has been postulated that polygalacturonase is significant in the infection of root hairs of leguminous plants by Rhizobium spp. Recently this theory has been strongly questioned. Evidence for polygalacturonase was based on methods which would not distinguish between this enzyme and other pectic glycosidases. The possibility that pectin lyase or polygalacturonate lyase is involved in the invasion of red clover by Rhizobium trifolii was investigated. Weak pectin lyase activity was detected in uninoculated seedlings, but no increase in the activity was produced in inoculated seedlings. It was concluded that neither of the lyases has significance in the infection process.

Characteristics of the immobilized pectin lyase activity from a commercial pectolytic enzyme preparation

1990 ◽  
Vol 10 (6) ◽  
pp. 531-539 ◽  
Author(s):  
P. Lozano ◽  
A. Manjón ◽  
J. L. Iborra ◽  
D. M. Gálvez
Keyword(s):  
Enzyme Preparation ◽  
Pectin Lyase ◽  
Lyase Activity ◽  
Pectolytic Enzyme

scholarly journals Periplasmic depolymerase provides insight into ABC transporter-dependent secretion of bacterial capsular polysaccharides

2018 ◽  
Vol 115 (21) ◽  
pp. E4870-E4879 ◽  
Author(s):  
Sean D. Liston ◽  
Stephen A. McMahon ◽  
Audrey Le Bas ◽  
Michael D. L. Suits ◽  
James H. Naismith ◽  
...  
Keyword(s):  
Cell Surface ◽  
Abc Transporter ◽  
Pectate Lyase ◽  
Capsular Polysaccharides ◽  
Ph Optimum ◽  
Pectate Lyases ◽  
Surface Assembly ◽  
Binding Groove ◽  
Biochemical Analyses ◽  
Vi Antigen

Capsules are surface layers of hydrated capsular polysaccharides (CPSs) produced by many bacteria. The human pathogenSalmonella entericaserovar Typhi produces “Vi antigen” CPS, which contributes to virulence. In a conserved strategy used by bacteria with diverse CPS structures, translocation of Vi antigen to the cell surface is driven by an ATP-binding cassette (ABC) transporter. These transporters are engaged in heterooligomeric complexes proposed to form an enclosed translocation conduit to the cell surface, allowing the transporter to power the entire process. We identified Vi antigen biosynthesis genetic loci in genera of theBurkholderiales, which are paradoxically distinguished fromS.Typhi by encoding VexL, a predicted pectate lyase homolog. Biochemical analyses demonstrated that VexL is an unusual metal-independent endolyase with an acidic pH optimum that is specific for O-acetylated Vi antigen. A 1.22-Å crystal structure of the VexL-Vi antigen complex revealed features which distinguish common secreted catabolic pectate lyases from periplasmic VexL, which participates in cell-surface assembly. VexL possesses a right-handed parallel β-superhelix, of which one face forms an electropositive glycan-binding groove with an extensive hydrogen bonding network that includes Vi antigen acetyl groups and confers substrate specificity. VexL provided a probe to interrogate conserved features of the ABC transporter-dependent export model. When introduced intoS. Typhi, VexL localized to the periplasm and degraded Vi antigen. In contrast, a cytosolic derivative had no effect unless export was disrupted. These data provide evidence that CPS assembled in ABC transporter-dependent systems is actually exposed to the periplasm during envelope translocation.

scholarly journals RNA chaperones Hfq and ProQ play a key role in the virulence of the plant pathogenic bacterium Dickeya dadantii

2021 ◽  
Author(s):  
Simon Leonard ◽  
Camille Villard ◽  
William Nasser ◽  
Sylvie Reverchon ◽  
Florence Hommais
Keyword(s):  
Extracellular Enzymes ◽  
Pectate Lyase ◽  
Soft Rot ◽  
Pathogenic Bacterium ◽  
Growth Defect ◽  
Dickeya Dadantii ◽  
Genes Encoding ◽  
Lyase Activity ◽  
Rna Chaperones ◽  
Post Transcriptional Regulation

Dickeya dadantii is an important pathogenic bacterium that infects a number of crops including potato and chicory. While extensive works have been carried out on the control of the transcription of its genes encoding the main virulence functions, little information is available on the post-transcriptional regulation of these functions. We investigated the involvement of the RNA chaperones Hfq and ProQ in the production of the main D. dadantii virulence functions. Phenotypic assays on the hfq and proQ mutants showed that inactivation of hfq resulted in a growth defect, a modified capacity for biofilm formation and strongly reduced motility, and in the production of degradative extracellular enzymes (proteases, cellulase and pectate lyases). Accordingly, the hfq mutant failed to cause soft rot on chicory leaves. The proQ mutant had reduced resistance to osmotic stress, reduced extracellular pectate lyase activity compared to the wild-type strain, and reduced virulence on chicory leaves. Most of the phenotypes of the hfq and proQ mutants were related to the low amounts of mRNA of the corresponding virulence factors. Complementation of the double mutant hfq-proQ by each individual protein and cross-complementation of each chaperone suggested that they might exert their effects via partially overlapping but different sets of targets. Overall, it clearly appeared that the two Hfq and ProQ RNA chaperones are important regulators of pathogenicity in D. dadantii. This underscores that virulence genes are regulated post transcriptionally by non-coding RNAs.

scholarly journals HrpW of Erwinia amylovora, a New Harpin That Contains a Domain Homologous to Pectate Lyases of a Distinct Class

1998 ◽  
Vol 180 (19) ◽  
pp. 5203-5210 ◽  
Author(s):  
Jihyun F. Kim ◽  
Steven V. Beer
Keyword(s):  
Plant Cell Wall ◽  
Erwinia Amylovora ◽  
Pectate Lyase ◽  
Hypersensitive Reaction ◽  
Host Tissue ◽  
Wild Type ◽  
Pectate Lyases ◽  
Heat Stable ◽  
Lyase Activity ◽  
Type Strains

ABSTRACT Harpins, such as HrpN of Erwinia amylovora, are extracellular glycine-rich proteins that elicit the hypersensitive reaction (HR). We identified hrpW of E. amylovora, which encodes a protein similar to known harpins in that it is acidic, rich in glycine and serine, and lacks cysteine. A putative HrpL-dependent promoter was identified upstream ofhrpW, and Western blot analysis of hrpL mutants indicated that the production of HrpW is regulated by hrpL. HrpW is secreted via the Hrp (type III) pathway based on analysis of wild-type strains and hrp secretion mutants. When infiltrated into plants, HrpW induced rapid tissue collapse, which required active plant metabolism. The HR-eliciting activity was heat stable and protease sensitive. Thus, we concluded that HrpW is a new harpin. HrpW of E. amylovora consists of two domains connected by a Pro and Ser-rich sequence. A fragment containing the N-terminal domain was sufficient to elicit the HR. Although no pectate lyase activity was detected, the C-terminal region of HrpW is homologous to pectate lyases of a unique class, suggesting that HrpW may be targeted to the plant cell wall. Southern analysis indicated that hrpW is conserved among several Erwiniaspecies, and hrpW, provided in trans, enhanced the HR-inducing ability of a hrpN mutant. However, HrpW did not increase the virulence of a hrpN mutant in host tissue, and hrpW mutants retained the wild-type ability to elicit the HR in nonhosts and to cause disease in hosts.

scholarly journals Arabidopsis thaliana Expresses Multiple Lines of Defense to Counterattack Erwinia chrysanthemi

2007 ◽  
Vol 20 (7) ◽  
pp. 794-805 ◽  
Author(s):  
Mathilde Fagard ◽  
Alia Dellagi ◽  
Camille Roux ◽  
Claude Périno ◽  
Martine Rigault ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Signaling Pathways ◽  
Oxidative Burst ◽  
Pectate Lyase ◽  
Erwinia Chrysanthemi ◽  
Secreted Proteins ◽  
Type Ii Secretion ◽  
Susceptible Host ◽  
Pectate Lyases ◽  
Lyase Activity

Many taxonomically diverse plant species are attacked by Erwinia chrysanthemi, a member of the causal agents of soft-rotting diseases. Symptom development is due to the collective action of pectin-degrading enzymes secreted by the bacterium through a type II secretion system (T2SS). Using Arabidopsis thaliana as a susceptible host, we show that plants respond to E. chrysanthemi 3937 by expressing cell-wall reactions, production of an oxidative burst, and activation of salicylic acid (SA) and jasmonic acid (JA) or ethylene (ET) signaling pathways. We found that the oxidative burst is mainly generated via the expression of the AtrbohD gene, constitutes a barrier of resistance to bacterial attack, and acts independently of the SA-mediated response. To determine the importance of T2SS-secreted proteins in elicitation of these defenses, we used a T2SS deficient mutant and purified enzymatic preparations of representative members of strain 3937 pectate lyase activity. The T2SS-secreted proteins were responsible only partially for the activation of SA and JA or ET signaling pathways observed after infection with the wild-type bacterium and were not involved in the expression of other identified defense reactions. Our study shows the differential role played by pectate lyases isoenzymes in this process and highlights the complexity of the host immune network, which is finely controlled by the bacterium.

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