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Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stress

•Proteome-wide identification of heat-induced protein sequestrations.•Determination of novel stress granule components including aa-tRNA-synthetases.•Discovery of nucleus-associated deposits containing ribosome biogenesis factors.•Sequestrations suggest downregulation of protein synthesis and riboso...

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Bibliographic Details
Published in:FEBS letters 2015-11, Vol.589 (23), p.3654-3664
Main Authors: Cherkasov, Valeria, Grousl, Tomas, Theer, Patrick, Vainshtein, Yevhen, Gläßer, Christine, Mongis, Cyril, Kramer, Günter, Stoecklin, Georg, Knop, Michael, Mogk, Axel, Bukau, Bernd
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Language:English
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Summary:•Proteome-wide identification of heat-induced protein sequestrations.•Determination of novel stress granule components including aa-tRNA-synthetases.•Discovery of nucleus-associated deposits containing ribosome biogenesis factors.•Sequestrations suggest downregulation of protein synthesis and ribosome production. Environmental stress causes the sequestration of proteins into insoluble deposits including cytoplasmic stress granules (SGs), containing mRNA and a variety of translation factors. Here we systematically identified proteins sequestered in Saccharomyces cerevisiae at 46°C by a SG co-localization screen and proteomic analysis of insoluble protein fractions. We identified novel SG components including essential aminoacyl-tRNA synthetases. Moreover, we discovered nucleus-associated deposits containing ribosome biogenesis factors. Our study suggests downregulation of cytosolic protein synthesis and nuclear ribosome production at multiple levels through heat shock induced protein sequestrations.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2015.10.010