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J. Biol. Chem., Vol. 280, Issue 31, 28761-28765, August 5, 2005

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Global Loss of Set1-mediated H3 Lys⁴ Trimethylation Is Associated with Silencing Defects in Saccharomyces cerevisiae^*

Ian M. Fingerman, Chia-Ling Wu, Bradley D. Wilson, and Scott D. Briggs¶

From the Department of Biochemistry and the Cancer Center, Purdue University, West Lafayette, Indiana 47907 and the Walther Cancer Institute, Indianapolis, Indiana 46202

Post-translational histone modifications, such as acetylation, phosphorylation, ubiquitination, and methylation, have been correlated with regulation of gene expression. In Saccharomyces cerevisiae, Set1 has been identified as the sole histone methyltransferase required for histone H3 lysine 4 (Lys⁴) methylation. Yeast cells that do not express Set1 have several apparent phenotypes, including slow growth and defects in telomere, HML, and rDNA silencing. However, the mechanism by which the Set1 methyltransferase mediates differential histone H3 methylation (mono-, di-, and tri-) is still not understood, and the involvement of domains or regions in Set1 contributing to H3 Lys⁴ methylation has not been well characterized. In this study, the N terminus of Set1 was shown to be important for global and gene specific histone H3 trimethylation. We show that Set1 trimethyl-defective mutants can rescue a set1 slow growth defect. In contrast, Set1 trimethyl mutants were defective in telomere, rDNA, HML, and HMR silencing. Taken together, these data suggest that histone H3 Lys⁴ trimethylation is required for proper silencing, while mono- and/or dimethylation is sufficient for cell growth.

Received for publication, March 7, 2005 , and in revised form, June 13, 2005.

^* This work was supported by the Walther Cancer Institute, Purdue Cancer Center, American Cancer Society Institutional Grant, Indiana Elks Charities, Inc., and the Purdue Department of Biochemistry. This is journal paper number 17682 from the Purdue University Agricultural Experiment Station. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ A Sidney Kimmel Scholar. To whom correspondence should be addressed: Dept. of Biochemistry, Purdue University, 175 S. University, West Lafayette, IN 47907. Tel.: 765-494-0112; Fax: 765-494-7897; E-mail: sdbriggs{at}purdue.edu.

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