Welker, Sylvia and Rudolph, Birgit and Frenzel, Elke and Hagn, Franz and Liebisch, Gerhard and Schmitz, Gerd and Scheuring, Johannes and Kerth, Andreas and Blume, Alfred and Weinkauf, Sevil and Haslbeck, Martin and Kessler, Horst and Buchner, Johannes (2010) Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function. MOLECULAR CELL, 39 (4). pp. 507-520. ISSN 1097-2765, 1097-4164
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HEAT-SHOCK-PROTEIN; SACCHAROMYCES-CEREVISIAE; MOLECULAR CHAPERONES; ALPHA-SYNUCLEIN; PARKINSONS-DISEASE; GLOBAL ANALYSIS; YEAST; EXPRESSION; INDUCTION; PEPTIDES; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Klinische Chemie und Laboratoriumsmedizin |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 15 Jul 2020 09:26 |
| Last Modified: | 15 Jul 2020 09:26 |
| URI: | https://pred.uni-regensburg.de/id/eprint/24307 |
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