%0 Journal Article
%@ 1083-351X
%A Haldar, Swati
%A Saini, Ashok
%A Nanda, Jagpreet S
%A Saini, Sharanjot
%A Singh, Jagmohan
%D 2011
%F open:484
%I ASBMB
%J The Journal of biological chemistry
%K Chromatin structureEpigeneticsGene silencingHistone deacetylaseHistone methylation
%N 11
%P 9308-20
%T Role of Swi6/HP1 self-association-mediated recruitment of Clr4/Suv39 in establishment and maintenance of heterochromatin in fission yeast.
%U http://crdd.osdd.net/open/484/
%V 286
%X 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.
%Z Copyright of this article belongs to ASBMB