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WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects

The metabolic complexity of living organisms relies on supramolecular protein structures which ensure vital processes, such as signal transduction, transcription, translation and cell wall synthesis. In eukaryotes WD40-repeat (WDR) proteins often function as molecular “hubs” mediating supramolecular...

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Autores principales: Guerriero, Gea, Hausman, Jean-Francois, Ezcurra, Inés
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4686805/
https://www.ncbi.nlm.nih.gov/pubmed/26734023
http://dx.doi.org/10.3389/fpls.2015.01112
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author Guerriero, Gea
Hausman, Jean-Francois
Ezcurra, Inés
author_facet Guerriero, Gea
Hausman, Jean-Francois
Ezcurra, Inés
author_sort Guerriero, Gea
collection PubMed
description The metabolic complexity of living organisms relies on supramolecular protein structures which ensure vital processes, such as signal transduction, transcription, translation and cell wall synthesis. In eukaryotes WD40-repeat (WDR) proteins often function as molecular “hubs” mediating supramolecular interactions. WDR proteins may display a variety of interacting partners and participate in the assembly of complexes involved in distinct cellular functions. In plants, the formation of lignocellulosic biomass involves extensive synthesis of cell wall polysaccharides, a process that requires the assembly of large transmembrane enzyme complexes, intensive vesicle trafficking, interactions with the cytoskeleton, and coordinated gene expression. Because of their function as supramolecular hubs, WDR proteins could participate in each or any of these steps, although to date only few WDR proteins have been linked to the cell wall by experimental evidence. Nevertheless, several potential cell wall-related WDR proteins were recently identified using in silico approaches, such as analyses of co-expression, interactome and conserved gene neighborhood. Notably, some WDR genes are frequently genomic neighbors of genes coding for GT2-family polysaccharide synthases in eukaryotes, and this WDR-GT2 collinear microsynteny is detected in diverse taxa. In angiosperms, two WDR genes are collinear to cellulose synthase genes, CesAs, whereas in ascomycetous fungi several WDR genes are adjacent to chitin synthase genes, chs. In this Perspective we summarize and discuss experimental and in silico studies on the possible involvement of WDR proteins in plant cell wall formation. The prospects of biotechnological engineering for enhanced biomass production are discussed.
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spelling pubmed-46868052016-01-05 WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects Guerriero, Gea Hausman, Jean-Francois Ezcurra, Inés Front Plant Sci Plant Science The metabolic complexity of living organisms relies on supramolecular protein structures which ensure vital processes, such as signal transduction, transcription, translation and cell wall synthesis. In eukaryotes WD40-repeat (WDR) proteins often function as molecular “hubs” mediating supramolecular interactions. WDR proteins may display a variety of interacting partners and participate in the assembly of complexes involved in distinct cellular functions. In plants, the formation of lignocellulosic biomass involves extensive synthesis of cell wall polysaccharides, a process that requires the assembly of large transmembrane enzyme complexes, intensive vesicle trafficking, interactions with the cytoskeleton, and coordinated gene expression. Because of their function as supramolecular hubs, WDR proteins could participate in each or any of these steps, although to date only few WDR proteins have been linked to the cell wall by experimental evidence. Nevertheless, several potential cell wall-related WDR proteins were recently identified using in silico approaches, such as analyses of co-expression, interactome and conserved gene neighborhood. Notably, some WDR genes are frequently genomic neighbors of genes coding for GT2-family polysaccharide synthases in eukaryotes, and this WDR-GT2 collinear microsynteny is detected in diverse taxa. In angiosperms, two WDR genes are collinear to cellulose synthase genes, CesAs, whereas in ascomycetous fungi several WDR genes are adjacent to chitin synthase genes, chs. In this Perspective we summarize and discuss experimental and in silico studies on the possible involvement of WDR proteins in plant cell wall formation. The prospects of biotechnological engineering for enhanced biomass production are discussed. Frontiers Media S.A. 2015-12-22 /pmc/articles/PMC4686805/ /pubmed/26734023 http://dx.doi.org/10.3389/fpls.2015.01112 Text en Copyright © 2015 Guerriero, Hausman and Ezcurra. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Guerriero, Gea
Hausman, Jean-Francois
Ezcurra, Inés
WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects
title WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects
title_full WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects
title_fullStr WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects
title_full_unstemmed WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects
title_short WD40-Repeat Proteins in Plant Cell Wall Formation: Current Evidence and Research Prospects
title_sort wd40-repeat proteins in plant cell wall formation: current evidence and research prospects
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4686805/
https://www.ncbi.nlm.nih.gov/pubmed/26734023
http://dx.doi.org/10.3389/fpls.2015.01112
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