Role of Swi6/HP1 self-association-mediated recruitment of Clr4/Suv39 in establishment and maintenance of heterochromatin in fission yeast.

Haldar, Swati and Saini, Ashok and Nanda, Jagpreet S and Saini, Sharanjot and Singh, Jagmohan (2011) Role of Swi6/HP1 self-association-mediated recruitment of Clr4/Suv39 in establishment and maintenance of heterochromatin in fission yeast. The Journal of biological chemistry, 286 (11). pp. 9308-20. ISSN 1083-351X

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Abstract

Swi6/HP1, an evolutionarily conserved protein, is critical for heterochromatin assembly in fission yeast and higher eukaryotes. In fission yeast, histone deacetylation by histone deacetylases is thought to be followed by H3-Lys-9 methylation by the histone methyltransferase Clr4/Suv39H1. H3-Lys-9-Me2 interacts with the chromodomain of Swi6/HP1. Swi6/HP1 is thought to act downstream of Clr4/Suv39, and further self-association of Swi6/HP1 is assumed to stabilize the heterochromatin structure. Here, we show that the self-association-defective mutant of Swi6 does not interact with Clr4. It not only fails to localize to heterochromatin loci but also interferes with heterochromatic localization of H3-Lys-9-Me2 (and thereby Clr4) and the endogenous Swi6 in a dominant negative manner. Thus, self-association of Swi6/HP1 helps in binding to and recruitment of Clr4 and thereby in establishment and maintenance of heterochromatin by a concerted rather than a sequential mechanism.

Item Type:	Article
Additional Information:	Copyright of this article belongs to ASBMB
Uncontrolled Keywords:	Chromatin structureEpigeneticsGene silencingHistone deacetylaseHistone methylation
Subjects:	Q Science > QD Chemistry
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	08 Dec 2011 18:56
Last Modified:	09 Jan 2015 09:13
URI:	http://crdd.osdd.net/open/id/eprint/484

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