| Literature DB >> 23142645 |
Yuichi Mishima1, Makoto Watanabe, Toru Kawakami, Chanika D Jayasinghe, Junji Otani, Yusuke Kikugawa, Masahiro Shirakawa, Hiroshi Kimura, Osamu Nishimura, Saburo Aimoto, Shoji Tajima, Isao Suetake.
Abstract
The majority of the genome in eukaryotes is packaged into transcriptionally inactive chromatin. Heterochromatin protein 1 (HP1) is a major player in the establishment and maintenance of heterochromatin. HP1 specifically recognizes a methylated lysine residue at position 9 in histone H3 through its N-terminal chromo domain (CD). To elucidate the binding properties of HP1α to nucleosomes in vitro, we reconstituted nucleosomes containing histone H3 trimethylated at lysine 9. HP1α exhibited high-affinity binding to nucleosomes containing methylated histone H3 in a nucleosome core-number-dependent manner. The hinge region (HR) connecting the CD and C-terminal chromoshadow domain (CSD), and the CSD contributed to the selective binding of HP1α to histone H3 with trimethylated lysine 9 through weak DNA binding and by suppressing the DNA binding, respectively. We propose that not only the specific recognition of lysine 9 methylation of histone H3 by the CD but also the HR and the CSD cooperatively contribute to the selective binding of HP1α to histone H3 lysine 9 methylated nucleosomes.Entities:
Mesh：
Substances：
Year: 2012 PMID： 23142645 DOI： 10.1016/j.jmb.2012.10.018
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469