The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains

Curr Genet. 2017 Feb;63(1):9-13. doi: 10.1007/s00294-016-0610-6. Epub 2016 May 26.

Abstract

Activation of the heterotrimeric kinase SNF1 via phosphorylation of a specific residue within the α subunit is essential for the release from glucose repression in the yeast Saccharomyces cerevisiae. When glucose is available, SNF1 is maintained in the dephosphorylated, inactive state by the phosphatase Glc7-Reg1. Recent findings suggest that Bmh and Ssb combine their unique client-binding properties to interact with the regulatory region of the SNF1 α subunit and by that stabilize a conformation of SNF1, which is accessible for Glc7-Reg1-dependent dephosphorylation. Together, the 14-3-3 protein Bmh and the Hsp70 homolog Ssb comprise a novel chaperone module, which is required to maintain proper glucose repression in the yeast S. cerevisiae.

Keywords: 14-3-3; AMPK; Bmh; Glc7; Hsp70; PKA; Reg1; SNF1; Saccharomyces cerevisiae; Ssb.

Publication types

  • Review

MeSH terms

  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • HSP72 Heat-Shock Proteins / chemistry
  • HSP72 Heat-Shock Proteins / metabolism*
  • Intrinsically Disordered Proteins / chemistry
  • Intrinsically Disordered Proteins / metabolism
  • Protein Binding
  • Protein Domains
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism
  • Yeasts / metabolism*

Substances

  • Fungal Proteins
  • HSP72 Heat-Shock Proteins
  • Intrinsically Disordered Proteins
  • Saccharomyces cerevisiae Proteins