Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Andrew J. Bannister, Philip Zegerman, Janet F. Partridge, Eric A. Miska, Jean O. Thomas, Robin C. Allshire and Tony Kouzarides ()
Additional contact information
Andrew J. Bannister: University of Cambridge
Philip Zegerman: University of Cambridge
Janet F. Partridge: MRC Human Genetics Unit, Western General Hospital
Eric A. Miska: University of Cambridge
Jean O. Thomas: University of Cambridge
Robin C. Allshire: MRC Human Genetics Unit, Western General Hospital
Tony Kouzarides: University of Cambridge

Nature, 2001, vol. 410, issue 6824, 120-124

Abstract: Abstract Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing1,2. The chromo domain of HP1 is necessary for both targeting and transcriptional repression3,4. In the fission yeast Schizosaccharomyces pombe, the correct localization of Swi6 (the HP1 equivalent) depends on Clr4, a homologue of the mammalian SUV39H1 histone methylase5,6. Both Clr4 and SUV39H1 methylate specifically lysine 9 of histone H3 (ref. 6). Here we show that HP1 can bind with high affinity to histone H3 methylated at lysine 9 but not at lysine 4. The chromo domain of HP1 is identified as its methyl-lysine-binding domain. A point mutation in the chromo domain, which destroys the gene silencing activity of HP1 in Drosophila3, abolishes methyl-lysine-binding activity. Genetic and biochemical analysis in S. pombe shows that the methylase activity of Clr4 is necessary for the correct localization of Swi6 at centromeric heterochromatin and for gene silencing. These results provide a stepwise model for the formation of a transcriptionally silent heterochromatin: SUV39H1 places a ‘methyl marker’ on histone H3, which is then recognized by HP1 through its chromo domain. This model may also explain the stable inheritance of the heterochromatic state.

Date: 2001
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DOI: 10.1038/35065138

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