Plant Physiology Preview
Published on April 9, 2002; 10.1104/pp.010720
Received August 10, 2001
Returned for revision November 21, 2001
Accepted January 17, 2002
Glucosylation Activity and Complex Formation of Two Classes of
Reversibly Glycosylated Polypeptides
Sandra M.J. Langeveld *, Marco Vennik , Marijke Kottenhagen , Ringo van Wijk , Ankie Buijk , Jan W. Kijne , and Sylvia de Pater
Department of Applied Plant Sciences of the Netherlands Organisation for Applied Scientific Research (S.M.J.L., M.V., M.K., R.v.W., A.B., S.d.P.) and Institute of Molecular Plant Sciences (J.W.K.), Center for Phytotechnology, Leiden University, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands
* Corresponding author; email: Langeveld{at}rulbim.leidenuniv.nl.
Reversibly glycosylated polypeptides (RGPs) have been implicated in polysaccharide biosynthesis. In plants, these proteins may function, for example, in cell wall synthesis and/or in synthesis of starch. We have isolated wheat (Triticum aestivum) and rice (Oryza sativa) Rgp cDNA clones to study the function of RGPs. Sequence comparisons showed the existence of two classes of RGP proteins, designated RGP1 and RGP2. Glucosylation activity of RGP1 and RGP2 from wheat and rice was studied. After separate expression of Rgp1 and Rgp2 in Escherichia coli or yeast (Saccharomyces cerevisiae), only RGP1 showed self-glucosylation. In Superose 12 fractions from wheat endosperm extract, a polypeptide with a molecular mass of about 40 kD is glucosylated by UDP-glucose. Transgenic tobacco (Nicotiana tabacum) plants, overexpressing either wheat Rgp1 or Rgp2, were generated. Subsequent glucosylation assays revealed that in RGP1-containing tobacco extracts as well as in RGP2-containing tobacco extracts UDP-glucose is incorporated, indicating that an RGP2-containing complex is active. Gel filtration experiments with wheat endosperm extracts and extracts from transgenic tobacco plants, overexpressing either wheat Rgp1 or Rgp2, showed the presence of RGP1 and RGP2 in high-molecular mass complexes. Yeast two-hybrid studies indicated that RGP1 and RGP2 form homo- and heterodimers. Screening of a cDNA library using the yeast two-hybrid system and purification of the complex by an antibody affinity column did not reveal the presence of other proteins in the RGP complexes. Taken together, these results suggest the presence of active RGP1 and RGP2 homo- and heteromultimers in wheat endosperm.
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