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CK 2‐dependent inhibitory phosphorylation is relieved by Ppt 1 phosphatase for the ethanol stress‐specific activation of Hsf 1 in S accharomyces cerevisiae
Author(s) -
Cho BoRam,
Lee Peter,
Hahn JiSook
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12660
Subject(s) - phosphorylation , dephosphorylation , psychological repression , biology , phosphatase , ethanol , microbiology and biotechnology , heat shock protein , hsf1 , heat shock , transcription factor , heat shock factor , biochemistry , hsp70 , gene expression , gene
Summary Ethanol, the major fermentation product of S accharomyces cerevisiae , has long been known as an inducer of heat shock response, but the underlying mechanisms by which ethanol activates heat shock transcription factor ( HSF ) are not well understood. We demonstrate that CK 2‐dependent phosphorylation on S 608 is an ethanol stress‐specific repression mechanism of Hsf 1, which does not affect the basal or heat‐induced activity of Hsf 1. This repression is relieved by dephosphorylation by Ppt 1 which directly interacts with Hsf 1 via its tetratricopeptide repeat ( TPR ) domain. In response to ethanol stress, PPT1 deletion and CK 2 overexpression exert synergistic inhibitory effects on Hsf 1 activation, whereas Hsf 1 S 608 A mutant shows enhanced activation. Therefore, regulation of the Hsf 1 S 608 phosphorylation status by reciprocal actions of CK 2 and Ppt 1 might play an important role to determine Hsf 1 sensitivity towards ethanol stress.