The b-subunits of the Snf1 kinase in Saccharomyces cerevisae, Gal83 and Sip2, but not Sip1 are redundant in glucose derepression and regulation of sterol biosynthesis
Journal article, 2010

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 β-subunit Snf1, a regulatory γ-subunit Snf4 and one of three possible β-subunits, Sip1, Sip2 or Gal83. We used a systematic approach to study the role of the three β-subunits by analysing all seven possible combinations of β-subunit deletions together with the reference strain. Previous studies showed that the three β-subunits are redundant for growth on alternative carbon sources. Here we report that the mutant strain with only SIP1 expressed (sip2Δ gal83Δ) 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. © 2010 Blackwell Publishing Ltd.


Jie Zhang

Chalmers, Chemical and Biological Engineering, Life Sciences

Lisbeth Olsson

Chalmers, Chemical and Biological Engineering, Industrial biotechnology

Jens B Nielsen

Chalmers, Chemical and Biological Engineering, Life Sciences

Molecular Microbiology

0950-382X (ISSN) 1365-2958 (eISSN)

Vol. 77 2 371-383


Basic sciences

Areas of Advance

Life Science Engineering (2010-2018)

Subject Categories

Bioinformatics and Systems Biology

Other Industrial Biotechnology



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