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

FEBS Lett. 2015 Nov 30;589(23):3654-64. doi: 10.1016/j.febslet.2015.10.010. Epub 2015 Oct 17.

Abstract

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.

Keywords: Chaperone; Heat shock; Protein sequestration; Ribosome biogenesis; Stress granule; Translation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytoplasm / metabolism
  • Heat-Shock Response*
  • Organelle Biogenesis*
  • Protein Transport
  • Proteomics*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Ribosomes / metabolism*
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae Proteins / biosynthesis*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Solubility

Substances

  • RNA, Messenger
  • Saccharomyces cerevisiae Proteins