Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly - PubMed (original) (raw)
. 2001 Apr 6;292(5514):110-3.
doi: 10.1126/science.1060118. Epub 2001 Mar 15.
Affiliations
- PMID: 11283354
- DOI: 10.1126/science.1060118
Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
J Nakayama et al. Science. 2001.
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 Lys9 methylation in vivo. Localization of Swi6, a homolog of Drosophila HP1, to heterochomatic regions is dependent on H3 Lys9 methylation. Moreover, an H3-specific deacetylase Clr3 and a beta-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.
Comment in
- Molecular biology. The histone modification circus.
Berger SL. Berger SL. Science. 2001 Apr 6;292(5514):64-5. Science. 2001. PMID: 11294220 No abstract available.
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