The S. pombe Translation Initiation Factor eIF4G Is Sumoylated and Associates with the SUMO Protease Ulp2.
Smith, Duncan L
AffiliationGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom.
MetadataShow full item record
AbstractSUMO 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 two translation initiation factors that we identified as co-purifying with Ulp2, eIF4G and eIF3h. We demonstrate that eIF4G, but not eIF3h, is sumoylated. This modification is increased under conditions that produce cytoplasmic stress granules. Consistent with this we observe partial co-localisation of eIF4G and SUMO in stressed cells. Using HeLa cells, we demonstrate that human eIF4GI is also sumoylated; in vitro studies indicate that human eIF4GI is modified on K1368 and K1588, that are located in the C-terminal eIF4A- and Mnk-binding sites respectively.
CitationThe S. pombe Translation Initiation Factor eIF4G Is Sumoylated and Associates with the SUMO Protease Ulp2. 2014, 9 (5):e94182 PLoS ONE
- Pli1(PIAS1) SUMO ligase protected by the nuclear pore-associated SUMO protease Ulp1SENP1/2.
- Authors: Nie M, Boddy MN
- Issue date: 2015 Sep 11
- The dynamics and mechanism of SUMO chain deconjugation by SUMO-specific proteases.
- Authors: Békés M, Prudden J, Srikumar T, Raught B, Boddy MN, Salvesen GS
- Issue date: 2011 Mar 25
- c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4.
- Authors: González-Prieto R, Cuijpers SA, Kumar R, Hendriks IA, Vertegaal AC
- Issue date: 2015
- Binding to small ubiquitin-like modifier and the nucleolar protein Csm1 regulates substrate specificity of the Ulp2 protease.
- Authors: de Albuquerque CP, Suhandynata RT, Carlson CR, Yuan WT, Zhou H
- Issue date: 2018 Aug 3
- In Vitro Studies Reveal a Sequential Mode of Chain Processing by the Yeast SUMO (Small Ubiquitin-related Modifier)-specific Protease Ulp2.
- Authors: Eckhoff J, Dohmen RJ
- Issue date: 2015 May 8