Hsp12 of S. cerevisiae is up-regulated several hundred-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, changes in cell morphology are observed 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, but in the presence of lipids, it adopts a well-defined structure with five amphipathic helical elements. The presence of Hsp12 does not alter the overall lipid composition of the plasma membrane but affects its organization and increases membrane stability.
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Hsp12 of S. cerevisiae is up-regulated several hundred-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, changes in cell morphology are observed 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...
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