Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function

Sylvia Welker, Birgit Rudolph, Elke Frenzel, Franz Hagn, Gerhard Liebisch, Gerd Schmitz, Johannes Scheuring, Andreas Kerth, Alfred Blume, Sevil Weinkauf, Martin Haslbeck, Horst Kessler, Johannes Buchner

Research output: Contribution to journalArticlepeer-review

128 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)507-520
Number of pages14
JournalMolecular Cell
Volume39
Issue number4
DOIs
StatePublished - Aug 2010

Keywords

  • Cellbio
  • Proteins

Fingerprint

Dive into the research topics of 'Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function'. Together they form a unique fingerprint.

Cite this