The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.

ABSTRACT: SUMO is a small post-translational modifier, that is attached to lysine residues in target proteins. It acts by altering protein-protein interactions, protein localisation and protein activity. SUMO chains can also act as substrates for ubiquitination, resulting in proteasome-mediated degradation of the target protein. SUMO is removed from target proteins by one of a number of specific proteases. The processes of sumoylation and desumoylation have well documented roles in DNA metabolism and in the maintenance of chromatin structure. To further analyse the role of this modification, we have purified protein complexes containing the S. pombe SUMO protease, Ulp2. These complexes contain proteins required for ribosome biogenesis, RNA stability and protein synthesis. Here we have focussed on tw

SUBMITTER: Jongjitwimol J 

PROVIDER: S-EPMC4018355 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature