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

被引：138

作者：

Welker, Sylvia ^{[1
]}

Rudolph, Birgit ^{[1
]}

Frenzel, Elke ^{[1
]}

Hagn, Franz ^{[1
]}

Liebisch, Gerhard ^{[3
]}

Schmitz, Gerd ^{[3
]}

Scheuring, Johannes ^{[1
]}

Kerth, Andreas ^{[4
]}

Blume, Alfred ^{[4
]}

Weinkauf, Sevil ^{[1
]}

Haslbeck, Martin ^{[1
]}

Kessler, Horst ^{[1
,2
]}

Buchner, Johannes ^{[1
]}

机构：

[1] Tech Univ Munich, Dept Chem, Munich Ctr Integrated Prot Sci, D-85747 Garching, Germany

[2] Tech Univ Munich, Dept Chem, Inst Adv Study, D-85747 Garching, Germany

[3] Univ Regensburg, Inst Clin Chem & Lab Med, D-93053 Regensburg, Germany

[4] Univ Halle Wittenberg, Inst Chem, D-06120 Halle, Germany

来源：

MOLECULAR CELL | 2010年 / 39卷 / 04期

关键词：

HEAT-SHOCK-PROTEIN; SACCHAROMYCES-CEREVISIAE; MOLECULAR CHAPERONES; ALPHA-SYNUCLEIN; PARKINSONS-DISEASE; GLOBAL ANALYSIS; YEAST; EXPRESSION; INDUCTION; PEPTIDES;

D O I：

10.1016/j.molcel.2010.08.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：507 / 520

页数：14

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