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

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...

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/92214a3ec7214f9bb813caae917cf735
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spelling	oai:doaj.org-article:92214a3ec7214f9bb813caae917cf7352021-11-18T08:19:48ZThe S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.1932-620310.1371/journal.pone.0094182https://doaj.org/article/92214a3ec7214f9bb813caae917cf7352014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24818994/?tool=EBIhttps://doaj.org/toc/1932-6203SUMO 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.Jirapas JongjitwimolMin FengLihong ZhouOliver WilkinsonLauren SmallRobert BaldockDeborah L TaylorDuncan SmithLucas D BowlerSimon J MorleyFelicity Z WattsPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 5, p e94182 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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 The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
description	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.
format	article
author	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
author_facet	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
author_sort	Jirapas Jongjitwimol
title	The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
title_short	The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
title_full	The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
title_fullStr	The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
title_full_unstemmed	The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
title_sort	s. pombe translation initiation factor eif4g is sumoylated and associates with the sumo protease ulp2.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/92214a3ec7214f9bb813caae917cf735
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The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.

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