Increasing Saccharomyces cerevisiae stress resistance, through the overactivation of the heat shock response resulting from defects in the Hsp90 chaperone, does not extend replicative life span but can be associated with slower chronological ageing of nondividing cells

Mol Genet Genomics. 2001 Apr;265(2):258-63. doi: 10.1007/s004380000409.


Recent studies on Drosophila and Caenorhabditis elegans indicate that increases in stress resistance result in a longer chronological life span, an effect that must operate primarily on the postmitotic tissues of the adult. Stress resistance can be increased through decreases in Hsp90 chaperone activity, since Hsp90 acts to downregulate the activity of heat shock transcription factor. This study investigated whether the increases in stress resistance associated with reduced Hsp90 chaperone activity influence ageing in the budding yeast Saccharomyces cerevisiae, ageing being measured either as the replicative (nonchronological) senescence of budding cells or as the chronological ageing of non-dividing (stationary phase) cultures. Overactivation of the heat shock response caused no slowing of replicative senescence. In some situations though it was associated with a longer chronological life span of stationary cells, the yeast equivalent of the postmitotic state. This is consistent with the idea that stress resistance exerts its life span-extending effects primarily in postmitotic cells and tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / metabolism
  • Cyclophilin D
  • Cyclophilins*
  • HSP90 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Response
  • Peptidylprolyl Isomerase / metabolism
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins


  • Carrier Proteins
  • Cyclophilin D
  • HSP82 protein, S cerevisiae
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Saccharomyces cerevisiae Proteins
  • Cyclophilins
  • Peptidylprolyl Isomerase