Title |
The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains
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Published in |
Current Genetics, May 2016
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DOI | 10.1007/s00294-016-0610-6 |
Pubmed ID | |
Authors |
Volker Hübscher, Kaivalya Mudholkar, Sabine Rospert |
Abstract |
Activation of the heterotrimeric kinase SNF1 via phosphorylation of a specific residue within the α subunit is essential for the release from glucose repression in the yeast Saccharomyces cerevisiae. When glucose is available, SNF1 is maintained in the dephosphorylated, inactive state by the phosphatase Glc7-Reg1. Recent findings suggest that Bmh and Ssb combine their unique client-binding properties to interact with the regulatory region of the SNF1 α subunit and by that stabilize a conformation of SNF1, which is accessible for Glc7-Reg1-dependent dephosphorylation. Together, the 14-3-3 protein Bmh and the Hsp70 homolog Ssb comprise a novel chaperone module, which is required to maintain proper glucose repression in the yeast S. cerevisiae. |
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Unknown | 2 | 100% |
Demographic breakdown
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Members of the public | 2 | 100% |
Mendeley readers
Geographical breakdown
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Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 9 | 33% |
Student > Master | 4 | 15% |
Student > Bachelor | 3 | 11% |
Researcher | 3 | 11% |
Student > Doctoral Student | 2 | 7% |
Other | 0 | 0% |
Unknown | 6 | 22% |
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Immunology and Microbiology | 1 | 4% |
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Unknown | 7 | 26% |