Titre :

The specificity of pectate lyase VdPelB from Verticilium dahliae is highlighted by structural, dynamical and biochemical characterizations

Auteur(s) :

Safran, Josip [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Ung, Vanessa [Auteur]
School of Chemical Sciences [Auckland]
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Habrylo, Olivier [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Molinié, Roland [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Fontaine, Jean-Xavier [Auteur]
Institut Charles Viollette (ICV) - ULR 7394
Lemaire, Adrien [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Voxeur, Aline [Auteur]
Université Paris Saclay (COmUE)
Pilard, Serge [Auteur]
Université de Picardie Jules Verne [UPJV]
Pau-Roblot, Corinne [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Mercadante, Davide [Auteur]
School of Chemical Sciences [Auckland]
Pelloux, Jérôme [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Sénéchal, Fabien [Auteur]
BioEcoAgro - UMR transfrontalière INRAe - UMRT1158
Safran, Josip [Auteur]

Titre de la revue :

International Journal of Biological Macromolecules

Nom court de la revue :

International Journal of Biological Macromolecules

Numéro :

231

Pagination :

123137

Éditeur :

Elsevier BV

Date de publication :

2023-03

ISSN :

0141-8130

Mot(s)-clé(s) en anglais :

Pectate lyase
Pectins
Homogalacturonan
Oligogalacturonides
Verticillium dahliae

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

Pectins, complex polysaccharides and major components of the plant primary cell wall, can be degraded by pectate lyases (PLs). PLs cleave glycosidic bonds of homogalacturonans (HG), the main pectic domain, by β-elimination, ...
Lire la suite >Pectins, complex polysaccharides and major components of the plant primary cell wall, can be degraded by pectate lyases (PLs). PLs cleave glycosidic bonds of homogalacturonans (HG), the main pectic domain, by β-elimination, releasing unsaturated oligogalacturonides (OGs). To understand the catalytic mechanism and structure/function of these enzymes, we characterized VdPelB from Verticillium dahliae. We first solved the crystal structure of VdPelB at 1.2 Å resolution showing that it is a right-handed parallel β-helix structure. Molecular dynamics (MD) simulations further highlighted the dynamics of the enzyme in complex with substrates that vary in their degree of methylesterification, identifying amino acids involved in substrate binding and cleavage of non-methylesterified pectins. We then biochemically characterized wild type and mutated forms of VdPelB. Pectate lyase VdPelB was most active on non-methylesterified pectins, at pH 8.0 in presence of Ca2+ ions. The VdPelB-G125R mutant was most active at pH 9.0 and showed higher relative activity compared to native enzyme. The OGs released by VdPelB differed to that of previously characterized PLs, showing its peculiar specificity in relation to its structure. OGs released from Verticillium-partially tolerant and sensitive flax cultivars differed which could facilitate the identification VdPelB-mediated elicitors of defence responses.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Computational Molecular Systems Biology

Date de dépôt :

2023-04-04T13:51:48Z
2023-04-05T09:05:28Z