Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.

In response to severe environmental stresses eukaryotic cells shut down translation and accumulate components of the translational machinery in stress granules (SGs). Since they contain mainly mRNA, translation initiation factors and 40S ribosomal subunits, they have been referred to as dominant acc...

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Autores principales:	Tomas Grousl, Pavel Ivanov, Ivana Malcova, Petr Pompach, Ivana Frydlova, Renata Slaba, Lenka Senohrabkova, Lenka Novakova, Jiri Hasek
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0f2cda6a202840abbdbebc51beb35bc6
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spelling	oai:doaj.org-article:0f2cda6a202840abbdbebc51beb35bc62021-11-18T07:56:08ZHeat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.1932-620310.1371/journal.pone.0057083https://doaj.org/article/0f2cda6a202840abbdbebc51beb35bc62013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23451152/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203In response to severe environmental stresses eukaryotic cells shut down translation and accumulate components of the translational machinery in stress granules (SGs). Since they contain mainly mRNA, translation initiation factors and 40S ribosomal subunits, they have been referred to as dominant accumulations of stalled translation preinitiation complexes. Here we present evidence that the robust heat shock-induced SGs of S. cerevisiae also contain translation elongation factors eEF3 (Yef3p) and eEF1Bγ2 (Tef4p) as well as translation termination factors eRF1 (Sup45p) and eRF3 (Sup35p). Despite the presence of the yeast prion protein Sup35 in heat shock-induced SGs, we found out that its prion-like domain is not involved in the SGs assembly. Factors eEF3, eEF1Bγ2 and eRF1 were accumulated and co-localized with Dcp2 foci even upon a milder heat shock at 42°C independently of P-bodies scaffolding proteins. We also show that eEF3 accumulations at 42°C determine sites of the genuine SGs assembly at 46°C. We suggest that identification of translation elongation and termination factors in SGs might help to understand the mechanism of the eIF2α factor phosphorylation-independent repression of translation and SGs assembly.Tomas GrouslPavel IvanovIvana MalcovaPetr PompachIvana FrydlovaRenata SlabaLenka SenohrabkovaLenka NovakovaJiri HasekPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 2, p e57083 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tomas Grousl Pavel Ivanov Ivana Malcova Petr Pompach Ivana Frydlova Renata Slaba Lenka Senohrabkova Lenka Novakova Jiri Hasek Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
description	In response to severe environmental stresses eukaryotic cells shut down translation and accumulate components of the translational machinery in stress granules (SGs). Since they contain mainly mRNA, translation initiation factors and 40S ribosomal subunits, they have been referred to as dominant accumulations of stalled translation preinitiation complexes. Here we present evidence that the robust heat shock-induced SGs of S. cerevisiae also contain translation elongation factors eEF3 (Yef3p) and eEF1Bγ2 (Tef4p) as well as translation termination factors eRF1 (Sup45p) and eRF3 (Sup35p). Despite the presence of the yeast prion protein Sup35 in heat shock-induced SGs, we found out that its prion-like domain is not involved in the SGs assembly. Factors eEF3, eEF1Bγ2 and eRF1 were accumulated and co-localized with Dcp2 foci even upon a milder heat shock at 42°C independently of P-bodies scaffolding proteins. We also show that eEF3 accumulations at 42°C determine sites of the genuine SGs assembly at 46°C. We suggest that identification of translation elongation and termination factors in SGs might help to understand the mechanism of the eIF2α factor phosphorylation-independent repression of translation and SGs assembly.
format	article
author	Tomas Grousl Pavel Ivanov Ivana Malcova Petr Pompach Ivana Frydlova Renata Slaba Lenka Senohrabkova Lenka Novakova Jiri Hasek
author_facet	Tomas Grousl Pavel Ivanov Ivana Malcova Petr Pompach Ivana Frydlova Renata Slaba Lenka Senohrabkova Lenka Novakova Jiri Hasek
author_sort	Tomas Grousl
title	Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
title_short	Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
title_full	Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
title_fullStr	Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
title_full_unstemmed	Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
title_sort	heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in s. cerevisiae.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/0f2cda6a202840abbdbebc51beb35bc6
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Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.

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