PLOS_J_Jongjitwimol_2014.pdf (2.93 MB)
The S. pombe translation initiation factor eIF4G is sumoylated and associates with the SUMO protease Ulp2
journal contribution
posted on 2023-06-08, 18:03 authored by Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L Taylor, Duncan Smith, Lucas Bowler, Simon Morley, Felicity WattsSUMO is a small post-translational modifier, that is attached to lysine residues in target proteins. It acts by altering proteinprotein 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.
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Publication status
- Published
File Version
- Published version
Journal
PLoS ONEISSN
1932-6203Publisher
Public Library of ScienceExternal DOI
Issue
5Volume
9Article number
e94182Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2014-08-07First Open Access (FOA) Date
2014-08-07First Compliant Deposit (FCD) Date
2014-08-07Usage metrics
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