Regulation of self-glycosylation of reversibly glycosylated polypeptides from Solarumtuberosum

PAMELA TESTASECCA; FLAVIA A. WALD; EUGENIA COZZARIN; SILVIA MORENO

PHYSIOLOGIA PLANTARUM

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 2004 vol. 121 p. 27 - 34

0031-9317

Reversibly glycosylated polypeptides (RGPs) belong to a family of self-glycosylating proteins believed to be involved in plant polysaccharide synthesis. The precise function of these enzymes remains to be elucidated. Our results showed that the RGP 38-kDa subunit is phosphorylated in potato extracts (Solanum tuberosum L.). An increase in the self-glycosylation of Solanum tuberosum RGP (StRGP) 38-kDa subunit was observed after alkaline phosphatase (AP) treatment. Our results suggest that phosphorylation of StRGP appears to regulate its self-glycosylation. It was determined that when the StRGP reaction was carried out in the presence of UDP-[14C]Glc as the sugar donor and then 1 mM UDP was added in a chase-out experiment, radioactive UDP-Glc was obtained indicating that StRGP reaction seems to be reversible. The anomeric configuration of transferred sugars to StRGP protein was also studied.