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

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

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Munich Center for Integrated Protein Science, Technische Universit√§t M√ľnchen, Department Chemie, Lichtenbergstrasse 4, 85747 Garching, Germany.


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.

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