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Plant and Cell Physiology Advance Access published online on October 15, 2007
Plant and Cell Physiology, doi:10.1093/pcp/pcm135
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

The irregular xylem9 Mutant Is Deficient in Xylan Xylosyltransferase Activity

Chanhui Lee1, Malcolm A. O'Neill2, Yoichi Tsumuraya3, Alan G. Darvill2 and Zheng-Hua Ye1,*

1 Department of Plant Biology, University of Georgia, Athens, GA 30602 USA
2 Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA
3 Division of Life Science, Graduate School of Science and Engineering, Saitama University, 255 Shimo-okubo, Sakura-ku, Saitama 338-8570, Japan

*Corresponding author: Dr. Zheng-Hua Ye,Department of Plant Biology, University of Georgia, 2502 Plant Sciences, Athens, GA 30602 Tel: 706 542 1832, Fax: 706 542 1805, E-mail: zhye{at}plantbio.uga.edu


  Abstract

Xylan is the second most abundant polysaccharide in dicot wood, thus elucidating xylan biosynthetic pathway is required to understand the mechanisms controlling wood formation. Genetic and chemical studies in Arabidopsis have implicated three genes, FRAGILE FIBER8 (FRA8), IRREGULAR XYLEM8 (IRX8) and IRREGULAR XYLEM9 (IRX9), in the biosynthesis of glucuronoxylan (GX), but the biochemical functions of the encoded proteins are not known. In this study, we determined the effect of the fra8, irx8 and irx9 mutations on the activities of xylan xylosyltransferase (XylT) and glucuronyltransferase (GlcAT). We show that microsomes isolated from the stems of wild-type Arabidopsis exhibit XylT and GlcAT activities in the presence of exogenous 1,4-linked ß-D-xylooligomers. Xylooligomers ranging in size from 2 to 6 can be used as acceptors by XylT to form xylooligosaccharides with up to 12 xylosyl residues. We provide evidence that the irx9 mutation results in a substantial reduction in XylT activity but has no discernible effect on GlcAT activity. By contrast, neither XylT nor GlcAT activity is affected by fra8 and irx8 mutations. Our results provide biochemical evidence that the irx9 mutation results in a deficiency in xylan XylT activity, thus leading to a defect in the elongation of xylan backbone.

Keywords: Arabidopsis - irregular xylem9 - glucuronyltransferase - xylan - xylosyltransferas

(Received September 7, 2007; Accepted October 6, 2007)
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