Document Detail


The beta-subunits of the Snf1 kinase in Saccharomyces cerevisiae, Gal83 and Sip2, but not Sip1, are redundant in glucose derepression and regulation of sterol biosynthesis.
MedLine Citation:
PMID:  20545859     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The conserved Snf1/AMP-activated protein kinase family is one of the central components in the nutrient sensing and regulation of the carbon metabolism in eukaryotes. It is also involved in several other processes such as stress resistance, invasive growth and ageing. Snf1 kinase is composed of a catalytic alpha-subunit Snf1, a regulatory gamma-subunit Snf4 and one of three possible beta-subunits, Sip1, Sip2 or Gal83. We used a systematic approach to study the role of the three beta-subunits by analysing all seven possible combinations of beta-subunit deletions together with the reference strain. Previous studies showed that the three beta-subunits are redundant for growth on alternative carbon sources. Here we report that the mutant strain with only SIP1 expressed (sip2Delta gal83Delta) could utilize acetate, but neither ethanol nor glycerol, as alternative carbon source. We also showed that Gal83 is the most important isoform not only for the growth on non-fermentable carbon sources, but also for regulation of ergosterol biosynthetic genes, under glucose-limited condition. Furthermore, we found that Sip2, but not Sip1, can take over when Gal83 is deleted, but to a lesser extent. However, Sip1 may be sufficient for some other processes such as regulation of the nitrogen metabolism and meiosis.
Authors:
Jie Zhang; Lisbeth Olsson; Jens Nielsen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-06-10
Journal Detail:
Title:  Molecular microbiology     Volume:  77     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-23     Completed Date:  2010-10-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  371-83     Citation Subset:  IM    
Affiliation:
Department of Chemical and Biological Engineering, Chalmers University of Technology, Kemivägen 10, Gothenburg, Sweden.
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MeSH Terms
Descriptor/Qualifier:
AMP-Activated Protein Kinases / genetics,  metabolism
Acetic Acid / metabolism
Ethanol / metabolism
Fermentation
Gene Deletion
Gene Expression Regulation, Fungal
Glucose / metabolism*
Glycerol / metabolism
Mutation
Oligonucleotide Array Sequence Analysis
Protein Isoforms / genetics,  metabolism
Protein-Serine-Threonine Kinases / genetics,  metabolism*
RNA, Fungal / genetics
Repressor Proteins / genetics,  metabolism*
Saccharomyces cerevisiae / enzymology*,  genetics,  growth & development
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Sterols / biosynthesis*
Trans-Activators / genetics,  metabolism*
Chemical
Reg. No./Substance:
0/GAL83 protein, S cerevisiae; 0/Protein Isoforms; 0/RNA, Fungal; 0/Repressor Proteins; 0/SIP2 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Sterols; 0/Trans-Activators; 50-99-7/Glucose; 56-81-5/Glycerol; 64-17-5/Ethanol; 64-19-7/Acetic Acid; EC 2.7.1.-/SNF1-related protein kinases; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/SIP1 protein, S cerevisiae

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