Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly

Nakayama, J., Rice, J. C., Strahl, B. D., Allis, C. D., Grewal, S. I. S. (2001) Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science, 292 (5514). pp. 110-113. ISSN 0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/11283354
DOI: 10.1126/science.1060118

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 Lys(9)) 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 Lys(9) methylation in vivo. Localization of Swi6, a homolog of Drosophila HP1, to heterochomatic regions is dependent on H3 Lysg methylation. Moreover, an H3-specific deacetylase Clr3 and a beta -propeller domain protein Rik1 are required for H3 Lys(9) 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.

Item Type: Paper
Uncontrolled Keywords: FISSION YEAST CHROMOSOME SEGREGATION PROTEIN ACETYLATION CENTROMERE CHROMATIN DOMAINS INHERITANCE DROSOPHILA MUTATIONS
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > Chromatin dynamics
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
CSHL Authors:
Communities: CSHL labs > Grewal lab
Depositing User: Matt Covey
Date Deposited: 17 Jan 2014 20:04
Last Modified: 17 Jan 2014 20:04
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29275

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