In vivo analysis of SUMOylated proteins from Drosophila melanogaster using improved strategies for expression, purification, and identification of conjugation sites

Abstract

SUMOylation is a post-translational modification characterized by the covalent and reversible binding of the Small Ubiquitin-like Modifier ( SUMO) to a target protein. SUMOylation regulates many cellular processes, including transcription, DNA damage repair, protein-protein interactions, protein localization and trafficking. We are interested on studying the in vivo role of Drosophila SUMO (Smt3) implicated in the steroid biosynthetic pathway and required for metamorphosis in flies. We are developing a novel strategy to isolate tissue specific SUMOylated proteins, based on the in vivo biotinylation of a variant of Smt3 (bioSUMO).