Open AccessSnf1-Like Protein Kinase Ssp2 Regulates Glucose Derepression in Schizosaccharomyces pombe
Author(s) -
T. Matsuzawa,
Yuka Fujita,
Hideki Tohda,
Kaoru Takegawa
Publication year - 2012
Publication title -
eukaryotic cell
Language(s) - English
Resource type - Journals
eISSN - 1535-9778
pISSN - 1535-9786
DOI - 10.1128/ec.05268-11
Subject(s) - derepression , snf3 , biology , schizosaccharomyces pombe , subcellular localization , phosphorylation , microbiology and biotechnology , transcription factor , mutant , psychological repression , cytoplasm , gene , biochemistry , saccharomyces cerevisiae , gene expression
The function of two fission yeast genes, SPCC74.03c/ssp2 + and SPAC23H4.02/ppk9 + , encoding an Snf1-like protein kinase were investigated. Deletion ofssp2 + caused a partial defect in glucose derepression ofinv1 + ,fbp1 + , andgld1 + and in assimilation of sucrose and glycerol, while a mutation inppk9 + had no apparent effect. Scr1, a transcription factor involved in glucose repression, localized to the nucleus under glucose-rich conditions and to the cytoplasm during glucose starvation in wild-type cells. In contrast, in thessp2 Δ mutant, Scr1 localized to the nucleus in cells grown in glucose-rich medium as well as in glucose-starved cells. Immunoblot analysis showed that Ssp2 is required for the phosphorylation of Scr1 upon glucose deprivation. Mutation of five putative Ssp2 recognition sites in Scr1 prevented glucose derepression of invertase in glucose-starved cells. These results indicate that Ssp2 regulates phosphorylation and subcellular localization of Scr1 in response to glucose.