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Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly

Science  06 Apr 2001:
Vol. 292, Issue 5514, pp. 110-113
DOI: 10.1126/science.1060118

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Abstract

The assembly of higher order chromatin structures has been linked to the covalent modifications of histone tails. We provide in vivo evidence that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast. Both the conserved chromo- and SET domains of Clr4 are required for H3 Lys9methylation in vivo. Localization of Swi6, a homolog ofDrosophila HP1, to heterochomatic regions is dependent on H3 Lys9 methylation. Moreover, an H3-specific deacetylase Clr3 and a β-propeller domain protein Rik1 are required for H3 Lys9 methylation by Clr4 and Swi6 localization. These data define a conserved pathway wherein sequential histone modifications establish a “histone code” essential for the epigenetic inheritance of heterochromatin assembly.

  • * To whom correspondence should be addressed. E-mail: grewal{at}cshl.org

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