Glycosyl transferases in family 61 mediate arabinofuranosyl transfer onto xylan in grasses

A - Papers appearing in refereed journals

Anders, N., Wilkinson, M. D., Lovegrove, A., Freeman, J., Tryfona, T., Pellny, T. K., Weimar, T., Mortimer, J. C., Stott, K., Baker, J. M., Defoin-Platel, M., Shewry, P. R., Dupree, P. and Mitchell, R. A. C. 2012. Glycosyl transferases in family 61 mediate arabinofuranosyl transfer onto xylan in grasses. Proceedings of the National Academy of Sciences of the United States of America. 109 (3), pp. 989-993.

AuthorsAnders, N., Wilkinson, M. D., Lovegrove, A., Freeman, J., Tryfona, T., Pellny, T. K., Weimar, T., Mortimer, J. C., Stott, K., Baker, J. M., Defoin-Platel, M., Shewry, P. R., Dupree, P. and Mitchell, R. A. C.
Abstract

Xylan, a hemicellulosic component of the plant cell wall, is one of the most abundant polysaccharides in nature. In contrast to dicots, xylan in grasses is extensively modified by α-(1,2)– and α-(1,3)–linked arabinofuranose. Despite the importance of grass arabinoxylan in human and animal nutrition and for bioenergy, the enzymes adding the arabinosyl substitutions are unknown. Here we demonstrate that knocking-down glycosyltransferase (GT) 61 expression in wheat endosperm strongly decreases α-(1,3)–linked arabinosyl substitution of xylan. Moreover, heterologous expression of wheat and rice GT61s in Arabidopsis leads to arabinosylation of the xylan, and therefore provides gain-of-function evidence for α-(1,3)-arabinosyltransferase activity. Thus, GT61 proteins play a key role in arabinoxylan biosynthesis and therefore in the evolutionary divergence of grass cell walls. 

KeywordsRRES175; 175_Biochemistry; 175_Climatology; 175_Plant sciences; 175_Genetics
Year of Publication2012
JournalProceedings of the National Academy of Sciences of the United States of America
Journal citation109 (3), pp. 989-993
Digital Object Identifier (DOI)doi:10.1073/pnas.1115858109
Open accessPublished as bronze (free) open access
Funder project or codeCGI
MCB
Publisher's version
Publication process dates
Accepted07 Dec 2011
PublisherNational Academy of Sciences
Copyright licensePublisher copyright

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