First published online December 23, 2005; 10.1104/pp.105.072744
Plant Physiology 140:49-58 (2006)
© 2006 American Society of Plant Biologists
BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES
ARABINAN DEFICIENT 1 Is a Putative Arabinosyltransferase Involved in Biosynthesis of Pectic Arabinan in Arabidopsis1,[W]
Jesper Harholt,
Jacob Krüger Jensen,
Susanne Oxenbøll Sørensen,
Caroline Orfila2,
Markus Pauly and
Henrik Vibe Scheller*
Plant Biochemistry Laboratory, Department of Plant Biology, the Royal Veterinary and Agricultural University, 40 Thorvaldsensvej, DK–1871 Frederiksberg C, Denmark (J.H., J.K.J., S.O.S., C.O., H.V.S.); and Max-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Golm, Germany (M.P.)
The function of a putative glycosyltransferase (At2g35100) was investigated in Arabidopsis (Arabidopsis thaliana). The protein is predicted to be a type 2 membrane protein with a signal anchor. Two independent mutant lines with T-DNA insertion in the ARABINAN DEFICIENT 1 (ARAD1) gene were analyzed. The gene was shown to be expressed in all tissues but particularly in vascular tissues of leaves and stems. Analysis of cell wall polysaccharides isolated from leaves and stems showed that arabinose content was reduced to about 75% and 46%, respectively, of wild-type levels. Immunohistochemical analysis indicated a specific decrease in arabinan with no change in other pectic domains or in glycoproteins. The cellular structure of the stem was also not altered. Isolated rhamnogalacturonan I from mutant tissues contained only about 30% of the wild-type amount of arabinose, confirming the specific deficiency in arabinan. Linkage analysis showed that the small amount of arabinan present in mutant tissue was structurally similar to that of the wild type. Transformation of mutant plants with the ARAD1 gene driven by the 35S promoter led to full complementation of the phenotype, but none of the transformants had more arabinan than the wild-type level. The data suggest that ARAD1 is an arabinan  -1,5-arabinosyltransferase. To our knowledge, the identification of other L-arabinosyltransferases has not been published.
1 This work was supported in part by the European Union (fifth framework contracts BIO4 CT97–2231) and the Danish National Research Foundation.
2 Present address: School of Applied Sciences, Northumbria University, Ellison Building, Ellison Place, Newcastle Upon Tyne NE1 8ST, UK.
The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Henrik Vibe Scheller (hvs{at}kvl.dk).
[W] The online version of this article contains Web-only data.
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.072744.
* Corresponding author; e-mail hvs{at}kvl.dk; fax 45–35283333.
Received October 11, 2005;
returned for revision November 27, 2005;
accepted November 28, 2005.
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