Science and Technology Production
Article
Authorship
De Pino V
;
Borán M
;
Norambuena L
;
González M
;
Reyes F,
;
Orellana A
;
MORENO, SILVIA
Date
2007
Publishing House and Editing Place
Springer Berlin
Magazine
PLANTA,
vol. 226
(pp. 335-345)
Springer Berlin
Summary
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Reversible glycosylated polypeptides (RGPs) are highly conserved plant-speciWc proteins, which can perform self-glycosylation. These proteins have beenshown essential in plants yet its precise function remains unknown. In order to understand the function of this self-glycosylating polypeptide, it is important to establish what factors are involved in the regulation of the RGP activity. Here we show that incubation at highionic strength produced a high self-glycosylation level and a high glycosy...
Reversible glycosylated polypeptides (RGPs) are highly conserved plant-speciWc proteins, which can perform self-glycosylation. These proteins have beenshown essential in plants yet its precise function remains unknown. In order to understand the function of this self-glycosylating polypeptide, it is important to establish what factors are involved in the regulation of the RGP activity. Here we show that incubation at highionic strength produced a high self-glycosylation level and a high glycosylation reversibility of RGP from Solanum tuberosum L. In contrast, incubation at low ionic strength led to a low level of glycosylation and a low glycosylation reversibility of RGP. The incubationat low ionic strength favored the formation of high molecular weight RGP-containing forms, whereas incubation at high ionic strength produced active RGPwith a molecular weight similar to the one expected for the monomer. Our data also showed that glycosylation of RGP, in its monomeric form, was highly reversible, whereas, a low reversibility of the protein glycosylation was observed when RGP was part of high molecular weight structures. In addition, glycosylation of RGP increased the occurrence of non-monomeric RGP-containing forms, suggesting that glycosylation may favor multimer formation. Finally, our results indicated that RGP from Arabidopsis thaliana and Pisum sativum are associated to golgi membranes, as part of protein complexes. A model for the regulation of the RGP activity and its binding to golgi membranes based on the glycosylation of the protein is proposed where the sugars linked to oligomeric form of RGP in the golgi may be Transferred to acceptors involved in polysaccharide biosynthesis.
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Key Words
POLYSACCHARIDE SYNTHESISCOMPLEX FORMATIONREVERSIBLE GLUCOSYLATED PROTEINUDP-SUGAR