The Saccharomyces cerevisiae protein Stm1p facilitates ribosome preservation during quiescence

Biochem Biophys Res Commun. 2013 Jan 11;430(2):745-50. doi: 10.1016/j.bbrc.2012.11.078. Epub 2012 Dec 1.

Abstract

Once cells exhaust nutrients from their environment, they enter an alternative resting state known as quiescence, whereby proliferation ceases and essential nutrients are obtained through internal stores and through the catabolism of existing macromolecules and organelles. One example of this is ribophagy, the degradation of ribosomes through the process of autophagy. However, some ribosomes need to be preserved for an anticipated recovery from nutrient deprivation. We found that the ribosome-associated protein Stm1p greatly increases the quantity of 80S ribosomes present in quiescent yeast cells and that these ribosomes facilitate increased protein synthesis rates once nutrients are restored. These findings suggest that Stm1p can act as a ribosome preservation factor under conditions of nutrient deprivation and restoration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Polyribosomes / metabolism*
  • Protein Biosynthesis
  • Ribosome Subunits, Large, Eukaryotic / metabolism*
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / growth & development*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sirolimus / pharmacology

Substances

  • DNA-Binding Proteins
  • Saccharomyces cerevisiae Proteins
  • Stm1 protein, S cerevisiae
  • Sirolimus