Snf1-Like Protein Kinase Ssp2 Regulates Glucose Derepression in Schizosaccharomyces pombe Tomohiko Matsuzawa a , Yasuko Fujita b , Hideki Tohda b and Kaoru Takegawa a a Department of Bioscience & Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan b ASPEX Division, Research Center, Asahi Glass Co., Ltd., Yokohama, Japan ABSTRACT The function of two fission yeast genes, SPCC74.03c/ ssp2 + and SPAC23H4.02/ ppk9 + , encoding an Snf1-like protein kinase were investigated. Deletion of ssp2 + caused a partial defect in glucose derepression of inv1 + , fbp1 + , and gld1 + and in assimilation of sucrose and glycerol, while a mutation in ppk9 + 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 the ssp2 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.
Snf1-Like Protein Kinase Ssp2 Regulates Glucose Derepression in Schizosaccharomyces pombe
Abstract
Snf1-Like Protein Kinase Ssp2 Regulates Glucose Derepression in Schizosaccharomyces pombe Tomohiko Matsuzawa a , Yasuko Fujita b , Hideki Tohda b and Kaoru Takegawa a a Department of Bioscience & Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan b ASPEX Division, Research Center, Asahi Glass Co., Ltd., Yokohama, Japan ABSTRACT The function of two fission yeast genes, SPCC74.03c/ ssp2 + and SPAC23H4.02/ ppk9 + , encoding an Snf1-like protein kinase were investigated. Deletion of ssp2 + caused a partial defect in glucose derepression of inv1 + , fbp1 + , and gld1 + and in assimilation of sucrose and glycerol, while a mutation in ppk9 + 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 the ssp2 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.Preview Only. This article cannot be rented because we do not currently have permission from the publisher.
/lp/american-society-for-microbiology/snf1-like-protein-kinase-ssp2-regulates-glucose-derepression-in-tt7E8LbsCH
Welcome to DeepDyve! Rent Premier Research Articles and Save Up to 90%
Preview Only
Snf1-Like Protein Kinase Ssp2 Regulates Glucose Derepression in Schizosaccharomyces pombe
Matsuzawa, Tomohiko; Fujita, Yasuko; Tohda, Hideki; Takegawa, Kaoru
Follow Eukaryotic Cell
, Volume 11 (2): 159
American Society For Microbiology – Feb 1, 2012
More Info
More Like This Article
View All dataSource[]=actageo&dataSource[]=aspet&dataSource[]=aaos&dataSource[]=aacc&dataSource[]=aacr&dataSource[]=aea&dataSource[]=aip&dataSource[]=ajnr&dataSource[]=ams&dataSource[]=aps_physical&dataSource[]=appi_book&dataSource[]=appi_journal&dataSource[]=apha&dataSource[]=asip&dataSource[]=asm&dataSource[]=asn&dataSource[]=aspb&dataSource[]=avs&dataSource[]=annual_reviews&dataSource[]=arxiv&dataSource[]=acm&dataSource[]=berghahn&dataSource[]=cabi&dataSource[]=clinical_trials&dataSource[]=dailymed&dataSource[]=degruyter&dataSource[]=du_press&dataSource[]=esa&dataSource[]=eu_press&dataSource[]=elsevier&dataSource[]=emerald&dataSource[]=ejtr&dataSource[]=emea&dataSource[]=epo&dataSource[]=faseb&dataSource[]=gsa&dataSource[]=health_affairs&dataSource[]=hindawi&dataSource[]=imanager&dataSource[]=imedpub&dataSource[]=informa_healthcare&dataSource[]=informs&dataSource[]=iop&dataSource[]=iucr&dataSource[]=iospress&dataSource[]=jbjs&dataSource[]=leftcoast&dataSource[]=lu_press&dataSource[]=mesharpe&dataSource[]=mary_ann_liebert&dataSource[]=medline&dataSource[]=mit_press&dataSource[]=nature&dataSource[]=oxford&dataSource[]=pier_professional&dataSource[]=pnas&dataSource[]=portlandpress&dataSource[]=psyc_articles&dataSource[]=psyc_books&dataSource[]=psyc_critiques&dataSource[]=plos_journal&dataSource[]=pubmed_central&dataSource[]=rsna&dataSource[]=rockefeller&dataSource[]=rcn&dataSource[]=ria&dataSource[]=rsc&dataSource[]=sage&dataSource[]=spie&dataSource[]=springer_journal&dataSource[]=springer&dataSource[]=taylor_francis&dataSource[]=aps&dataSource[]=the_scientist&dataSource[]=uc_press&dataSource[]=uspto_abstract&dataSource[]=wiley&dataSource[]=pct
© 2012 DeepDyve, Inc. All rights reserved.
Terms of Service | Privacy Policy
