Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function
| Autor: | Horst Kessler, Franz Hagn, Sylvia Welker, Martin Haslbeck, Alfred Blume, Sevil Weinkauf, Gerhard Liebisch, Elke Frenzel, Andreas Kerth, Johannes Scheuring, Birgit Rudolph, Johannes Buchner, Gerd Schmitz |
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| Rok vydání: | 2010 |
| Předmět: |
Protein Folding
Vesicle-associated membrane protein 8 Saccharomyces cerevisiae Proteins Morphology (linguistics) Genotype Membrane Fluidity Cell Saccharomyces cerevisiae Biology Protein Structure Secondary Stress (mechanics) Membrane Lipids Structure-Activity Relationship Cytosol Downregulation and upregulation Osmotic Pressure Stress Physiological Gene Expression Regulation Fungal medicine Molecular Biology Heat-Shock Proteins Sequence Deletion Cell Membrane Peripheral membrane protein Cell Biology Cell biology Oxidative Stress Protein Transport Phenotype medicine.anatomical_structure Membrane Heat-Shock Response |
| Zdroj: | Molecular Cell. 39(4):507-520 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2010.08.001 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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