Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function

Mol Cell. 2010 Aug 27;39(4):507-20. doi: 10.1016/j.molcel.2010.08.001.


Hsp12 of S. cerevisiae is upregulated several 100-fold in response to stress. Our phenotypic analysis showed that this protein is important for survival of a variety of stress conditions, including high temperature. In the absence of Hsp12, we observed changes in cell morphology under stress conditions. Surprisingly, in the cell, Hsp12 exists both as a soluble cytosolic protein and associated to the plasma membrane. The in vitro analysis revealed that Hsp12, unlike all other Hsps studied so far, is completely unfolded; however, in the presence of certain lipids, it adopts a helical structure. The presence of Hsp12 does not alter the overall lipid composition of the plasma membrane but increases membrane stability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Cytosol / metabolism
  • Gene Expression Regulation, Fungal
  • Genotype
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Response
  • Membrane Fluidity*
  • Membrane Lipids / metabolism
  • Osmotic Pressure
  • Oxidative Stress
  • Phenotype
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Transport
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Sequence Deletion
  • Stress, Physiological
  • Structure-Activity Relationship


  • HSP12 protein, S cerevisiae
  • Heat-Shock Proteins
  • Membrane Lipids
  • Saccharomyces cerevisiae Proteins