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

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• 作者：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 Buchn
• 刊名：Molecular Cell
• 出版年：2010
• 出版时间：27 August 2010
• 年：2010
• 卷：39
• 期：4
• 页码：507-520
• 全文大小：1563 K

文摘

Summary

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.