New insights into the specificity and processivity of two novel pectinases from Verticillium dahliae.

Show simple item record

dc.contributor.author Safran, Josip
dc.contributor.author Habrylo, Olivier
dc.contributor.author Cherkaoui, Mehdi
dc.contributor.author Lecomte, Sylvain
dc.contributor.author Voxeur, Aline
dc.contributor.author Pilard, Serge
dc.contributor.author Bassard, Solène
dc.contributor.author Pau-Roblot, Corinne
dc.contributor.author Mercadante, Davide
dc.contributor.author Pelloux, Jérôme
dc.contributor.author Sénéchal, Fabien
dc.coverage.spatial Netherlands
dc.date.accessioned 2021-06-22T02:37:53Z
dc.date.available 2021-06-22T02:37:53Z
dc.date.issued 2021-4
dc.identifier.issn 0141-8130
dc.identifier.uri https://hdl.handle.net/2292/55386
dc.description.abstract Pectin, the major non-cellulosic component of primary cell wall can be degraded by polygalacturonases (PGs) and pectin methylesterases (PMEs) during pathogen attack on plants. We characterized two novel enzymes, VdPG2 and VdPME1, from the fungal plant pathogen Verticillium dahliae. VdPME1 was most active on citrus methylesterified pectin (55-70%) at pH 6 and a temperature of 40 °C, while VdPG2 was most active on polygalacturonic acid at pH 5 and a temperature of 50 °C. Using LC-MS/MS oligoprofiling, and various pectins, the mode of action of VdPME1 and VdPG2 were determined. VdPME1 was shown to be processive, in accordance with the electrostatic potential of the enzyme. VdPG2 was identified as endo-PG releasing both methylesterified and non-methylesterified oligogalacturonides (OGs). Additionally, when flax roots were used as substrate, acetylated OGs were detected. The comparisons of OGs released from Verticillium-susceptible and partially resistant flax cultivars identified new possible elicitor of plant defence responses.
dc.format.medium Print-Electronic
dc.language eng
dc.publisher Elsevier BV
dc.relation.ispartofseries International journal of biological macromolecules
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher.
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm
dc.subject Flax
dc.subject Oligogalacturonides
dc.subject Pectin
dc.subject Pectin methylesterase
dc.subject Polygalacturonase
dc.subject Verticillium dahliae
dc.subject 0601 Biochemistry and Cell Biology
dc.title New insights into the specificity and processivity of two novel pectinases from Verticillium dahliae.
dc.type Journal Article
dc.identifier.doi 10.1016/j.ijbiomac.2021.02.035
pubs.begin-page 165
pubs.volume 176
dc.date.updated 2021-06-01T03:12:45Z
dc.rights.holder Copyright: The author en
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/33561463
pubs.end-page 176
pubs.publication-status Published
dc.rights.accessrights http://purl.org/eprint/accessRights/RetrictedAccess en
pubs.subtype Journal Article
pubs.elements-id 842674
dc.identifier.eissn 1879-0003
dc.identifier.pii S0141-8130(21)00310-X


Files in this item

Find Full text

This item appears in the following Collection(s)

Show simple item record

Share

Search ResearchSpace


Browse

Statistics