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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• 作者：Volker Hübscher ; Kaivalya Mudholkar ; Sabine Rospert
• 关键词：Saccharomyces cerevisiae ; 14 ; 3 ; 3 ; Bmh ; Hsp70 ; Ssb ; SNF1 ; AMPK ; Glc7 ; Reg1 ; PKA
• 刊名：Current Genetics
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：63
• 期：1
• 页码：9-13
• 全文大小：1000KB
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Microbial Genetics and Genomics; Microbiology; Biochemistry, general; Cell Biology; Plant Sciences; Proteomics;
• 出版者：Springer Berlin Heidelberg
• ISSN：1432-0983
• 卷排序：63

文摘

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.