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

Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L Taylor, Duncan Smith, Lucas D Bowler, Simon J Morley, Felicity Z Watts

Research output: Contribution to journalArticle

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 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.

Original languageEnglish
Pages (from-to)e94182
JournalPLoS One
Volume9
Issue number5
DOIs
Publication statusPublished - 2014
Externally publishedYes

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Peptide Initiation Factors
Schizosaccharomyces
translation (genetics)
Peptide Hydrolases
proteinases
Proteins
proteins
protein-protein interactions
modifiers (genes)
proteasome endopeptidase complex
ribosomes
in vitro studies
Sumoylation
Cytoplasmic Granules
chromatin
binding sites
granules
lysine
protein synthesis
Ubiquitination

Cite this

Jongjitwimol, Jirapas ; Feng, Min ; Zhou, Lihong ; Wilkinson, Oliver ; Small, Lauren ; Baldock, Robert ; Taylor, Deborah L ; Smith, Duncan ; Bowler, Lucas D ; Morley, Simon J ; Watts, Felicity Z. / The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2. In: PLoS One. 2014 ; Vol. 9, No. 5. pp. e94182.
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Jongjitwimol, J, Feng, M, Zhou, L, Wilkinson, O, Small, L, Baldock, R, Taylor, DL, Smith, D, Bowler, LD, Morley, SJ & Watts, FZ 2014, 'The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2' PLoS One, vol. 9, no. 5, pp. e94182. https://doi.org/10.1371/journal.pone.0094182

The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2. / Jongjitwimol, Jirapas; Feng, Min; Zhou, Lihong; Wilkinson, Oliver; Small, Lauren; Baldock, Robert; Taylor, Deborah L; Smith, Duncan; Bowler, Lucas D; Morley, Simon J; Watts, Felicity Z.

In: PLoS One, Vol. 9, No. 5, 2014, p. e94182.

Research output: Contribution to journalArticle

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T1 - The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2

AU - Jongjitwimol, Jirapas

AU - Feng, Min

AU - Zhou, Lihong

AU - Wilkinson, Oliver

AU - Small, Lauren

AU - Baldock, Robert

AU - Taylor, Deborah L

AU - Smith, Duncan

AU - Bowler, Lucas D

AU - Morley, Simon J

AU - Watts, Felicity Z

PY - 2014

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AB - 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 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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DO - 10.1371/journal.pone.0094182

M3 - Article

VL - 9

SP - e94182

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SN - 1932-6203

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