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Arabidopsis thaliana IRX 10 and two related proteins from psyllium and P hyscomitrella patens are xylan xylosyltransferases
Author(s) -
Jensen Jacob Krüger,
Johnson Nathan Robert,
Wilkerson Curtis Gene
Publication year - 2014
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12641
Subject(s) - xylan , arabidopsis thaliana , biochemistry , xylose , chemistry , heterologous expression , gene , biology , recombinant dna , polysaccharide , fermentation , mutant
Summary The enzymatic mechanism that governs the synthesis of the xylan backbone polymer, a linear chain of xylose residues connected by β‐1,4 glycosidic linkages, has remained elusive. Xylan is a major constituent of many kinds of plant cell walls, and genetic studies have identified multiple genes that affect xylan formation. In this study, we investigate several homologs of one of these previously identified xylan‐related genes, IRX 10 from A rabidopsis thaliana , by heterologous expression and in vitro xylan xylosyltransferase assay. We find that an IRX 10 homolog from the moss P hyscomitrella patens displays robust activity, and we show that the xylosidic linkage formed is a β‐1,4 linkage, establishing this protein as a xylan β‐1,4‐xylosyltransferase. We also find lower but reproducible xylan xylosyltransferase activity with A . thaliana IRX 10 and with a homolog from the dicot plant P lantago ovata , showing that xylan xylosyltransferase activity is conserved over large evolutionary distance for these proteins.