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Adolf-Butenandt Institut, University of Munich, Schillerstr. 44, 80336 Muenchen Germany
* To whom correspondence should be addressed. Email:
Imhof{at}lmu.de.
A large portion of the eukaryotic genome is packaged into transcriptionally silent heterochromatin. Several factors have been identified that play important roles during the establishment and maintenance of this condensed form. Methylation of lysine 9 within histone H3 and the subsequent binding of the chromo-domain protein HP1 is thought to initiate heterochromatin formation in vivo and to propagate a heterochromatic state through several cell divisions. Here we analysed the binding of HP1 to methylated chromatin in a fully reconstituted system. In contrast to its strong binding to methylated peptides, HP1 only weakly binds to methylated chromatin. However, the addition of recombinant SU(VAR) proteins such as ACF1 or SU(VAR)3-9 facilitates HP1 binding to chromatin methylated at H3K9. We propose that HP1 has multiple target sites that contribute to its recognition of chromatin only one of them being H3K9me. These findings have implications for the mechanisms of how specific chromatin modifications are recognized in vivo.
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
HP1 binding to chromatin methylated at H3K9 is enhanced by auxiliary factors
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Abstract
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