Structure of the SET domain histone lysine methyltransferase Clr4

Min, J. R., Zhang, X., Cheng, X. D., Grewal, S. I. S., Xu, R. M. (November 2002) Structure of the SET domain histone lysine methyltransferase Clr4. Nature Structural Biology, 9 (11). pp. 828-832. ISSN 1072-8368

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.

Item Type:	Paper
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes bioinformatics > genomics and proteomics > genetics & nucleic acid processing > epigenetics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > epigenetics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
Communities:	CSHL labs > Grewal lab CSHL labs > Xu lab
Depositing User:	Matt Covey
Date:	November 2002
Date Deposited:	14 Nov 2013 20:16
Last Modified:	14 Nov 2013 20:21
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/28748

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