Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function

Essays Biochem. 2023 Sep 13;67(5):781-795. doi: 10.1042/EBC20220224.

Abstract

Yeast is a valuable model organism for their ease of genetic manipulation, rapid growth rate, and relative similarity to higher eukaryotes. Historically, Saccharomyces cerevisiae has played a major role in discovering the function of complex proteins and pathways that are important for human health and disease. Heat shock protein 90 (Hsp90) is a molecular chaperone responsible for the stabilization and activation of hundreds of integral members of the cellular signaling network. Much important structural and functional work, including many seminal discoveries in Hsp90 biology are the direct result of work carried out in S. cerevisiae. Here, we have provided a brief overview of the S. cerevisiae model system and described how this eukaryotic model organism has been successfully applied to the study of Hsp90 chaperone function.

Keywords: Saccharomyces cerevisiae; heat shock proteins; molecular chaperones; post translational modification.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • HSP90 Heat-Shock Proteins / chemistry
  • Humans
  • Molecular Chaperones / genetics
  • Saccharomyces cerevisiae Proteins* / metabolism
  • Saccharomyces cerevisiae* / metabolism

Substances

  • Molecular Chaperones
  • HSP90 Heat-Shock Proteins
  • Saccharomyces cerevisiae Proteins