Premium
A new approach to study site‐specific protein sumoylation (925.3)
Author(s) -
Albuquerque Claudio,
Yeung Eyan,
Ma Shawn,
Fu Ting,
Zhou Huilin
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.925.3
Subject(s) - sumo protein , saccharomyces cerevisiae , sumo enzymes , proteome , lysine , ubiquitin , microbiology and biotechnology , biology , computational biology , yeast , chemistry , biochemistry , gene , amino acid
Protein sumoylation is a reversible post‐translational modification that regulates nuclear processes including gene transcription, nuclear transport and DNA repair. Like ubiquitin, SUMO is attached to the lysine side chains of target proteins via a cascade of E1‐activating, E2‐conjugating, and E3‐ligating enzymes, and it is removed by SUMO‐specific isopeptidases. Hundreds of proteins are known to be sumoylated in the yeast saccharomyces cerevisiae, however, relatively little is known about the precise sumoylation site(s) of most proteins. This is due to a lack of suitable method to map sumoylation sites in vivo. As a result, the function of sumoylation has remained mysterious in most cases. We have recently identified a novel role of protein sumoylation in preventing genome rearrangements and developed proteome‐wide approach to identify and quantify sumoylated proteins. Here we will report a new proteome‐wide method for the identification of site‐specific sumoylation in yeast, which greatly expanded the current knowledge of protein sumoylation. In addition, we will describe new approaches for the analysis of protein sumoylation in vitro. Results will be presented on the functional analysis of sumyolation of the sumoylation enzymes in yeast. Grant Funding Source : LICR