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Molecular and Cellular Biology, March 2002, p. 1298-1306, Vol. 22, No. 5
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.5.1298-1306.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Set2 Is a Nucleosomal Histone H3-Selective Methyltransferase That Mediates Transcriptional Repression

Brian D. Strahl,1,{dagger} Patrick A. Grant,1 Scott D. Briggs,1 Zu-Wen Sun,1 James R. Bone,1 Jennifer A. Caldwell,2 Sahana Mollah,2 Richard G. Cook,3 Jeffrey Shabanowitz,2 Donald F. Hunt,2,4 and C. David Allis1*

Department of Biochemistry and Molecular Genetics,1 Department of Pathology, University of Virginia Health System,4 Department of Chemistry, University of Virginia, Charlottesville, Virginia 22908,2 Department of Immunology, Baylor College of Medicine, Houston, Texas 770303

Received 11 September 2001/ Returned for modification 29 October 2001/ Accepted 28 November 2001

Recent studies of histone methylation have yielded fundamental new insights pertaining to the role of this modification in gene activation as well as in gene silencing. While a number of methylation sites are known to occur on histones, only limited information exists regarding the relevant enzymes that mediate these methylation events. We thus sought to identify native histone methyltransferase (HMT) activities from Saccharomyces cerevisiae. Here, we describe the biochemical purification and characterization of Set2, a novel HMT that is site-specific for lysine 36 (Lys36) of the H3 tail. Using an antiserum directed against Lys36 methylation in H3, we show that Set2, via its SET domain, is responsible for methylation at this site in vivo. Tethering of Set2 to a heterologous promoter reveals that Set2 represses transcription, and part of this repression is mediated through the HMT activity of the SET domain. These results suggest that Set2 and methylation at H3 Lys36 play a role in the repression of gene transcription.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908. Phone: (804) 243-6048. Fax: (804) 924-5069. E-mail: allis{at}virginia.edu.

{dagger} Present address: Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.

Molecular and Cellular Biology, March 2002, p. 1298-1306, Vol. 22, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.5.1298-1306.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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