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Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
Jun-ichi Nakayama,1Judd C. Rice,2Brian D. Strahl,2C. David Allis,2Shiv I. S. Grewal1*
The assembly of higher order chromatin structures has been linked
to the covalent modifications of histone tails. We providein vivo
evidence that lysine 9 of histone H3 (H3 Lys9) is
preferentially methylated by the Clr4 protein at
heterochromatin-associatedregions in fission yeast. Both the conserved
chromo- and SET domainsof Clr4 are required for H3 Lys9
methylation in vivo. Localization of Swi6, a homolog of
DrosophilaHP1, to heterochomatic regions is dependent on H3
Lys9 methylation. Moreover, an H3-specific deacetylase Clr3
and a-propeller domain protein Rik1 are required for H3
Lys9 methylation by Clr4 and Swi6 localization. These data
definea conserved pathway wherein sequential histone modifications
establisha "histone code" essential for the epigenetic inheritance
of heterochromatinassembly.
1 Cold Spring Harbor Laboratory, Post Office
Box 100, Cold Spring Harbor, NY 11724, USA.
2 Department of Biochemistry and Molecular Genetics,
University of Virginia, Charlottesville, VA 22908, USA.
*
To whom correspondence should be addressed. E-mail:
grewal{at}cshl.org
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Shelley L. Berger (6 April 2001) Science292 (5514), 64.
[DOI: 10.1126/science.1060028] |Summary »|Full Text »
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