Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/134461
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Type: Journal article
Title: Broad specific xyloglucan:xyloglucosyl transferases are formidable players in the re-modelling of plant cell wall structures
Author: Hrmova, M.
Stratilová, B.
Stratilová, E.
Citation: International Journal of Molecular Sciences, 2022; 23(3):1656-1-1656-19
Publisher: MDPI AG
Issue Date: 2022
ISSN: 1422-0067
1422-0067
Statement of
Responsibility: 
Maria Hrmova, Barbora Stratilová and Eva Stratilová
Abstract: Plant xyloglucan:xyloglucosyl transferases, known as xyloglucan endo-transglycosylases (XETs) are the key players that underlie plant cell wall dynamics and mechanics. These fundamental roles are central for the assembly and modifications of cell walls during embryogenesis, vegetative and reproductive growth, and adaptations to living environments under biotic and abiotic (environmental) stresses. XET enzymes (EC 2.4.1.207) have the β-sandwich architecture and the β-jelly-roll topology, and are classified in the glycoside hydrolase family 16 based on their evolutionary history. XET enzymes catalyse transglycosylation reactions with xyloglucan (XG)-derived and other than XG-derived donors and acceptors, and this poly-specificity originates from the structural plasticity and evolutionary diversification that has evolved through expansion and duplication. In phyletic groups, XETs form the gene families that are differentially expressed in organs and tissues in time- and space-dependent manners, and in response to environmental conditions. Here, we examine higher plant XET enzymes and dissect how their exclusively carbohydrate-linked transglycosylation catalytic function inter-connects complex plant cell wall components. Further, we discuss progress in technologies that advance the knowledge of plant cell walls and how this knowledge defines the roles of XETs. We construe that the broad specificity of the plant XETs underscores their roles in continuous cell wall restructuring and re-modelling.
Keywords: Crystal structures; evolutionary history; glycoside hydrolase family 16; mechanism of catalysis; molecular modelling and dynamics; transglycosylation reactions; substrate binding
Rights: © 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
DOI: 10.3390/ijms23031656
Grant ID: http://purl.org/au-research/grants/arc/DP120100900
Published version: http://dx.doi.org/10.3390/ijms23031656
Appears in Collections:Agriculture, Food and Wine publications

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