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Molecular and Cellular Biology, December 2005, p. 10566-10579, Vol. 25, No. 23
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.23.10566-10579.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Histone H3 Ser10 Phosphorylation-Independent Function of Snf1 and Reg1 Proteins Rescues a gcn5– Mutant in HIS3 Expression

Yang Liu,1 Xinjing Xu,2 Soumya Singh-Rodriguez,2 Yan Zhao,2 and Min-Hao Kuo1,2*

Program in Genetics,1 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 488242

Received 22 August 2005/ Accepted 14 September 2005

Gcn5 protein is a prototypical histone acetyltransferase that controls transcription of multiple yeast genes. To identify molecular functions that act downstream of or in parallel with Gcn5 protein, we screened for suppressors that rescue the transcriptional defects of HIS3 caused by a catalytically inactive mutant Gcn5, the E173H mutant. One bypass of Gcn5 requirement gene (BGR) suppressor was mapped to the REG1 locus that encodes a semidominant mutant truncated after amino acid 740. Reg1(1-740) protein does not rescue the complete knockout of GCN5, nor does it suppress other gcn5– defects, including the inability to utilize nonglucose carbon sources. Reg1(1-740) enhances HIS3 transcription while HIS3 promoter remains hypoacetylated, indicating that a noncatalytic function of Gcn5 is targeted by this suppressor protein. Reg1 protein is a major regulator of Snf1 kinase that phosphorylates Ser10 of histone H3. However, whereas Snf1 protein is important for HIS3 expression, replacing Ser10 of H3 with alanine or glutamate neither attenuates nor augments the BGR phenotypes. Overproduction of Snf1 protein also preferentially rescues the E173H allele. Biochemically, both Snf1 and Reg1(1-740) proteins copurify with Gcn5 protein. Snf1 can phosphorylate recombinant Gcn5 in vitro. Together, these data suggest that Reg1 and Snf1 proteins function in an H3 phosphorylation-independent pathway that also involves a noncatalytic role played by Gcn5 protein.

* Corresponding author. Mailing address: 401 BCH Building, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824. Phone: (517) 355-0163. Fax: (517) 353-9334. E-mail: kuom{at}msu.edu.

Molecular and Cellular Biology, December 2005, p. 10566-10579, Vol. 25, No. 23
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.23.10566-10579.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Shirra, M. K., McCartney, R. R., Zhang, C., Shokat, K. M., Schmidt, M. C., Arndt, K. M. (2008). A Chemical Genomics Study Identifies Snf1 as a Repressor of GCN4 Translation. J. Biol. Chem. 283: 35889-35898 [Abstract] [Full Text]  


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