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. 2002 Nov;9(11):828-32.
doi: 10.1038/nsb860.

Structure of the SET domain histone lysine methyltransferase Clr4

Jinrong Min  1 , Xing Zhang, Xiaodong Cheng, Shiv I S Grewal, Rui-Ming Xu
Affiliations

Structure of the SET domain histone lysine methyltransferase Clr4

Jinrong Min et al. Nat Struct Biol. 2002 Nov.

Abstract

Methylation of histone H3 lysine 9 is an important component of the 'histone code' for heterochromatic gene silencing. The SET domain-containing Clr4 protein, a close relative of Su(var)3-9 proteins in higher eukaryotes, specifically methylates lysine 9 of histone H3 and is essential for silencing in Schizosaccharomyces pombe. Here we report the 2.3 A resolution crystal structure of the catalytic domain of Clr4. The structure reveals an overall fold rich in beta-strands, a potential active site consisting of a SAM-binding pocket, and a connected groove that could accommodate the binding of the N-terminal tail of histone H3. The pre-SET motif contains a triangular zinc cluster coordinated by nine cysteines distant from the active site, whereas the post-SET region is largely flexible but proximal to the active site. The structure provides insights into the architecture of SET domain histone methyltransferases and establishes a paradigm for further characterization of the Clr4 family of epigenetic regulators.

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