Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
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DOI：
10.1371/journal.pone.0057083
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Hasek J
中科院分区：
文献类型：
--
作者：
Grousl T;Ivanov P;Malcova I;Pompach P;Frydlova I;Slaba R;Senohrabkova L;Novakova L;Hasek J
在严重的环境胁迫下，真核细胞会关闭翻译，并在应激颗粒（SGs）中积累翻译机制的组成部分。由于它们主要含有mRNA、翻译起始因子和40S核糖体亚基，因此被认为是停滞的翻译前起始复合物的显性积累。在这里，我们提出的证据表明，强大的热冲击诱导的SG的S。酿酒酵母还含有翻译延伸因子eEF 3（Yef3p）和eEF 1B γ2（Tf 4p）以及翻译终止因子eRF 1（Sup45p）和eRF 3（Sup35p）。尽管存在的酵母朊病毒蛋白Sup35在热休克诱导的SGs，我们发现，它的朊病毒样结构域是不参与的SGs组装。即使在42°C下较温和的热休克后，因子eEF 3、eEF 1B γ2和eRF 1也与Dcp 2灶聚集并共定位，与P体支架蛋白无关。我们还表明，eEF 3在42°C下的积累决定了46°C下真正SGs组装的位点。我们认为，鉴定SGs中的翻译延伸和终止因子可能有助于理解eIF2α因子磷酸化非依赖性抑制翻译和SGs组装的机制。
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.
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