MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
MCB.01055-07v1
27/22/7895    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Soontorngun, N.
Right arrow Articles by Turcotte, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Soontorngun, N.
Right arrow Articles by Turcotte, B.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2007, p. 7895-7905, Vol. 27, No. 22
0270-7306/07/$08.00+0     doi:10.1128/MCB.01055-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Regulation of Gluconeogenesis in Saccharomyces cerevisiae Is Mediated by Activator and Repressor Functions of Rds2{triangledown}

Nitnipa Soontorngun,2 Marc Larochelle,1 Simon Drouin,4 François Robert,4 and Bernard Turcotte1,2,3*

Departments of Medicine,1 Biochemistry,2 Microbiology and Immunology, Royal Victoria Hospital, McGill University, Montréal, Québec, Canada H3A 1A1,3 Institut de Recherches Cliniques de Montréal, Montréal, Québec, Canada H2W 1R74

Received 14 June 2007/ Returned for modification 16 August 2007/ Accepted 31 August 2007

In Saccharomyces cerevisiae, RDS2 encodes a zinc cluster transcription factor with unknown function. Here, we unravel a key function of Rds2 in gluconeogenesis using chromatin immunoprecipitation-chip technology. While we observed that Rds2 binds to only a few promoters in glucose-containing medium, it binds many additional genes when the medium is shifted to ethanol, a nonfermentable carbon source. Interestingly, many of these genes are involved in gluconeogenesis, the tricarboxylic acid cycle, and the glyoxylate cycle. Importantly, we show that Rds2 has a dual function: it directly activates the expression of gluconeogenic structural genes while it represses the expression of negative regulators of this pathway. We also show that the purified DNA binding domain of Rds2 binds in vitro to carbon source response elements found in the promoters of target genes. Finally, we show that upon a shift to ethanol, Rds2 activation is correlated with its hyperphosphorylation by the Snf1 kinase. In summary, we have characterized Rds2 as a novel major regulator of gluconeogenesis.

* Corresponding author. Mailing address: Department of Medicine, Room H7.83, Royal Victoria Hospital, McGill University, 687 Pine Ave. West, Montréal, Québec, Canada H3A 1A1. Phone: (514) 934-1934, ext. 35046. Fax: (514) 982-0893. E-mail: bernard.turcotte{at}mcgill.ca

{triangledown} Published ahead of print on 17 September 2007.

Molecular and Cellular Biology, November 2007, p. 7895-7905, Vol. 27, No. 22
0270-7306/07/$08.00+0     doi:10.1128/MCB.01055-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2007 by the American Society for Microbiology. All rights reserved.