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Your search keyword '"Pau-Roblot, Corinne"' showing total 12 results
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12 results on '"Pau-Roblot, Corinne"'

4. Capsular Polysaccharide Production in Bacteria of the Mycoplasma Genus: A Huge Diversity of Pathways and Synthases for So‐Called Minimal Bacteria.

Author

Vastel, Manon, Pau‐Roblot, Corinne, Ferré, Séverine, Tocqueville, Véronique, Ambroset, Chloé, Marois‐Créhan, Corinne, Gautier‐Bouchardon, Anne V., Tardy, Florence, and Gaurivaud, Patrice

Subjects
*POLYSACCHARIDES, *COLONIZATION (Ecology), *MYCOPLASMATALES, *MYCOPLASMA, *SYNTHASES
Abstract

Mycoplasmas are wall‐less bacteria with many species spread across various animal hosts in which they can be pathogenic. Despite their reduced anabolic capacity, some mycoplasmas are known to secrete hetero‐ and homopolysaccharides, which play a role in host colonization through biofilm formation or immune evasion, for instance. This study explores how widespread the phenomenon of capsular homopolysaccharide secretion is within mycoplasmas, and investigates the diversity of both the molecules produced and the synthase‐type glycosyltransferases responsible for their production. Fourteen strains representing 14 (sub)species from four types of hosts were tested in vitro for their polysaccharide secretion using both specific (immunodetection) and nonspecific (sugar dosage) assays. We evidenced a new, atypical homopolymer of β‐(1 → 6)‐glucofuranose (named glucofuranan) in the human pathogen Mycoplasma (M.) fermentans, as well as a β‐(1 → 6)‐glucopyranose polymer for the turkey pathogen M. iowae and galactan (β‐(1 → 6)‐galactofuranose) and β‐(1 → 2)‐glucopyranose for M. bovigenitalium infecting ruminants. Sequence and phylogenetic analyses revealed a huge diversity of synthases from varied Mycoplasma species. The clustering of these membrane‐embedded glycosyltransferases into three main groups was only partially correlated to the structure of the produced homopolysaccharides. [ABSTRACT FROM AUTHOR]

Published
2024
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5. Mutation of AtPME2, a pH-Dependent Pectin Methylesterase, Affects Cell Wall Structure and Hypocotyl Elongation

Author

Hocq, Ludivine, primary, Habrylo, Olivier, additional, Sénéchal, Fabien, additional, Voxeur, Aline, additional, Pau-Roblot, Corinne, additional, Safran, Josip, additional, Fournet, Françoise, additional, Bassard, Solène, additional, Battu, Virginie, additional, Demailly, Hervé, additional, Tovar, José C, additional, Pilard, Serge, additional, Marcelo, Paulo, additional, Savary, Brett J, additional, Mercadante, Davide, additional, Njo, Maria Fransiska, additional, Beeckman, Tom, additional, Boudaoud, Arezki, additional, Gutierrez, Laurent, additional, Pelloux, Jérôme, additional, and Lefebvre, Valérie, additional

Published
2023
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6. Mutation of AtPME2, a pH-Dependent Pectin Methylesterase, Affects Cell Wall Structure and Hypocotyl Elongation.

Author

Hocq, Ludivine, Habrylo, Olivier, Sénéchal, Fabien, Voxeur, Aline, Pau-Roblot, Corinne, Safran, Josip, Fournet, Françoise, Bassard, Solène, Battu, Virginie, Demailly, Hervé, Tovar, José C, Pilard, Serge, Marcelo, Paulo, Savary, Brett J, Mercadante, Davide, Njo, Maria Fransiska, Beeckman, Tom, Boudaoud, Arezki, Gutierrez, Laurent, and Pelloux, Jérôme

Subjects
PECTINESTERASE, PECTINS, CELLULAR mechanics, CELL anatomy, ENZYME specificity, PICHIA pastoris
Abstract

Pectin methylesterases (PMEs) modify homogalacturonan's chemistry and play a key role in regulating primary cell wall mechanical properties. Here, we report on Arabidopsis AtPME2 , which we found to be highly expressed during lateral root emergence and dark-grown hypocotyl elongation. We showed that dark-grown hypocotyl elongation was reduced in knock-out mutant lines as compared to the control. The latter was related to the decreased total PME activity as well as increased stiffness of the cell wall in the apical part of the hypocotyl. To relate phenotypic analyses to the biochemical specificity of the enzyme, we produced the mature active enzyme using heterologous expression in Pichia pastoris and characterized it through the use of a generic plant PME antiserum. AtPME2 is more active at neutral compared to acidic pH, on pectins with a degree of 55–70% methylesterification. We further showed that the mode of action of AtPME2 can vary according to pH, from high processivity (at pH8) to low processivity (at pH5), and relate these observations to the differences in electrostatic potential of the protein. Our study brings insights into how the pH-dependent regulation by PME activity could affect the pectin structure and associated cell wall mechanical properties. [ABSTRACT FROM AUTHOR]

Published
2024
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7. Plant polygalacturonase structures specify enzyme dynamics and processivities to fine-tune cell wall pectins

Author

Safran, Josip, primary, Tabi, Wafae, additional, Ung, Vanessa, additional, Lemaire, Adrien, additional, Habrylo, Olivier, additional, Bouckaert, Julie, additional, Rouffle, Maxime, additional, Voxeur, Aline, additional, Pongrac, Paula, additional, Bassard, Solène, additional, Molinié, Roland, additional, Fontaine, Jean-Xavier, additional, Pilard, Serge, additional, Pau-Roblot, Corinne, additional, Bonnin, Estelle, additional, Larsen, Danaé Sonja, additional, Morel-Rouhier, Mélanie, additional, Girardet, Jean-Michel, additional, Lefebvre, Valérie, additional, Sénéchal, Fabien, additional, Mercadante, Davide, additional, and Pelloux, Jérôme, additional

Published
2023
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10. The structural, dynamical and biochemical characterizations ofVerticillium dahliaepectate lyase, VdPelB, highlight its specificities

Author

Safran, Josip, primary, Ung, Vanessa, additional, Bouckaert, Julie, additional, Habrylo, Olivier, additional, Molinié, Roland, additional, Fontaine, Jean-Xavier, additional, Lemaire, Adrien, additional, Voxeur, Aline, additional, Pilard, Serge, additional, Pau-Roblot, Corinne, additional, Mercadante, Davide, additional, Pelloux, Jérôme, additional, and Sénéchal, Fabien, additional

Published
2022
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11. Differences in the structure of plant polygalacturonases specify enzymes’ dynamics and processivities to fine-tune pectins and root development

Author

Safran, Josip, Tabi, Wafae, Ung, Vanessa, Lemaire, Adrien, Habrylo, Olivier, Bouckaert, Julie, Rouffle, Maxime, Voxeur, Aline, Pongrac, Paula, Bassard, Solène, Molinié, Roland, Fontaine, Jean-Xavier, Pilard, Serge, Pau-Roblot, Corinne, Bonnin, Estelle, Larsen, Danaé Sonja, Morel-Rouhier, Mélanie, Girardet, Jean-Michel, Lefebvre, Valérie, Sénéchal, Fabien, Mercadante, Davide, Pelloux, Jérôme, Transfrontalière BioEcoAgro - UMR 1158 (BioEcoAgro), Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL), School of Chemical Sciences [Auckland], University of Auckland [Auckland], Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Plateforme Analytique (PFA), Université de Picardie Jules Verne (UPJV), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Interactions Arbres-Microorganismes (IAM), and Université de Lorraine (UL)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)

Subjects
[SDV]Life Sciences [q-bio], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology
Abstract

Corresponding authors:21 Jérôme Pelloux (jerome.pelloux@u-picardie.fr)22 Davide Mercadante (davide.mercadante@auckland.ac.nz)23 Fabien Sénéchal (fabien.senechal@u-picardie.fr); The fine-tuning of pectins by polygalacturonases (PGs) plays a key role in modulating plant cell wall chemistry and mechanics, impacting plant development. The high number of plant PG isoforms and their absence of inhibition by endogenous PG-Inhibiting Proteins (PGIPs) question the regulation of pectin depolymerization during development. Our understanding of the diversity and of the regulation of plant PGs has been impaired by the lack of protein structures. Here we resolved the crystal structures of two PGs from Arabidopsis, PGLR and ADPG2, whose expression overlap in roots and determined why plant PGs are not inhibited by PGIPs. By combining molecular dynamic simulations, analysis of enzymes’ kinetics and hydrolysis products, we showed that subtle differences in PGLR and ADPG2 structures translated into distinct dynamics and processivities. This leads to peculiar effects on root development, as determined by exogenous applications of enzymes.

Published
2022

12. Differences in the structure of plant polygalacturonases specify enzymes’ dynamics and processivities to fine-tune cell wall pectins

Author

Safran, Josip, primary, Tabi, Wafae, additional, Ung, Vanessa, additional, Lemaire, Adrien, additional, Habrylo, Olivier, additional, Bouckaert, Julie, additional, Rouffle, Maxime, additional, Voxeur, Aline, additional, Pongrac, Paula, additional, Bassard, Solène, additional, Molinié, Roland, additional, Fontaine, Jean-Xavier, additional, Pilard, Serge, additional, Pau-Roblot, Corinne, additional, Bonnin, Estelle, additional, Larsen, Danaé Sonja, additional, Morel-Rouhier, Mélanie, additional, Girardet, Jean-Michel, additional, Lefebvre, Valérie, additional, Sénéchal, Fabien, additional, Mercadante, Davide, additional, and Pelloux, Jérôme, additional

Published
2022
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