Reversible Glycosylated polypeptide is differentially expressed in plants

VERÓNICA DE PINO; DIEGO GRINMAN; SILVIA MORENO

Mar del Plata

Congreso; XLIII Reunión de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2007

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular

REVERSIBLE GLYCOSYLATED POLYPEPTIDE IS DIFFERENTIAL EXPRESSED IN PLANTS De Pino, V. Diego Grinman. and Moreno, S. Fundación Instituto Leloir, IIBBA-CONICET, Patricias Argentinas 435, (1405), Cap. Fed, Argentina. E-mail: VDePino@leloir.org.ar Reversible glycosylated polypeptides (RGPs) are highly conserved plant specific proteins, essential in plants and they perform self-glycosylation. Its precise function remains unknown. Here, we report features of RGP expression and activity regulation. Using specific probes for two RGP proteins, RGP1 and RGP2 thought to be involved in different metabolic pathways, we demonstrated a differential expression pattern. RGP1 is expressed earlier than RGP2 during plant development. Also, hormonal induction of RGP protein in a sugar mobilization context such as stress and elongation may happen. To establish what factors are involved in the regulation of the RGP activity, complex formation was reported earlier. Now, we show that these complexes are active since are capable of perform self glycosylation. Interestingly, their presence depends on the plant development stage, almost in rice. Complex formation modulates the RGP self glycosylation activity. To summarize, all data suggest that RGPs have a critical function in plants and show that are more than reversibly glycosylated polypeptides. Reversible glycosylated polypeptides (RGPs) are highly conserved plant specific proteins, essential in plants and they perform self-glycosylation. Its precise function remains unknown. Here, we report features of RGP expression and activity regulation. Using specific probes for two RGP proteins, RGP1 and RGP2 thought to be involved in different metabolic pathways, we demonstrated a differential expression pattern. RGP1 is expressed earlier than RGP2 during plant development. Also, hormonal induction of RGP protein in a sugar mobilization context such as stress and elongation may happen. To establish what factors are involved in the regulation of the RGP activity, complex formation was reported earlier. Now, we show that these complexes are active since are capable of perform self glycosylation. Interestingly, their presence depends on the plant development stage, almost in rice. Complex formation modulates the RGP self glycosylation activity. To summarize, all data suggest that RGPs have a critical function in plants and show that are more than reversibly glycosylated polypeptides.