An Arabidopsis gene encoding an α-xylosyltransferase involved in xyloglucan biosynthesis
TLDR
It is reported that etiolated pea microsomes contain an α-xylosyltransferase that catalyzes the transfer of xylose from UDP-[14C]xylose onto β(1,4)-linked glucan chains, and it is concluded that this Arabidopsis gene encodes an β-glucan synthase activity involved in xyloglucan biosynthesis.Abstract:
Microsomal membranes catalyze the formation of xyloglucan from UDP-Glc and UDP-Xyl by cooperative action of α-xylosyltransferase and β-glucan synthase activities. Here we report that etiolated pea microsomes contain an α-xylosyltransferase that catalyzes the transfer of xylose from UDP-[14C]xylose onto β(1,4)-linked glucan chains. The solubilized enzyme had the capacity to transfer xylosyl residues onto cello-oligosaccharides having 5 or more glucose residues. Analysis of the data from these biochemical assays led to the identification of a group of Arabidopsis genes and the hypothesis that one or more members of this group may encode α-xylosyltransferases involved in xyloglucan biosynthesis. To evaluate this hypothesis, the candidate genes were expressed in Pichia pastoris and their activities measured with the biochemical assay described above. One of the candidate genes showed cello-oligosaccharide-dependent xylosyltransferase activity. Characterization of the radiolabeled products obtained with cellopentaose as acceptor indicated that the pea and the Arabidopsis enzymes transfer the 14C-labeled xylose mainly to the second glucose residue from the nonreducing end. Enzymatic digestion of these radiolabeled products produced results that would be expected if the xylose was attached in an α(1,6)-linkage to the glucan chain. We conclude that this Arabidopsis gene encodes an α-xylosyltransferase activity involved in xyloglucan biosynthesis.read more
Citations
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Cell‐wall carbohydrates and their modification as a resource for biofuels
Markus Pauly,Kenneth Keegstra +1 more
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Disrupting Two Arabidopsis thaliana Xylosyltransferase Genes Results in Plants Deficient in Xyloglucan, a Major Primary Cell Wall Component
David Cavalier,Olivier Lerouxel,Lutz Neumetzler,Kazuchika Yamauchi,Antje Reinecke,Glenn Freshour,Olga A. Zabotina,Michael G. Hahn,Ingo Burgert,Markus Pauly,Markus Pauly,Natasha V. Raikhel,Kenneth Keegstra +12 more
TL;DR: It is concluded that XXT1 and XXT2 encode xylosyltransferases that are required for xyloglucan biosynthesis in vivo and this results in significant changes in the mechanical properties of these plants.
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Wheat arabinoxylans : Exploiting variation in amount and composition to develop enhanced varieties
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Guar Seed ß-Mannan Synthase Is a Member of the Cellulose Synthase Super Gene Family
Kanwarpal S. Dhugga,Roberto Barreiro,Brad Whitten,Kevin L. Stecca,Jan Hazebroek,Gursharn S. Randhawa,Maureen Dolan,Anthony J. Kinney,Dwight T. Tomes,Scott E. Nichols,Paul C. Anderson +10 more
TL;DR: The isolation of a complementary DNA (cDNA) clone encodingone such enzyme, mannan synthase (ManS), that makes the β-1, 4-mannan backbone of galactomannan, a hemicellulosic storage polysaccharide in guar seed endosperm walls is reported.
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Localization of Organelle Proteins by Isotope Tagging (LOPIT)
TL;DR: A proteomics method for determining the subcellular localization of membrane proteins in both the endoplasmic reticulum and the Golgi apparatus in Arabidopsis using a new tool for high-throughput protein localization by isotope tagging.
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