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MeCP2 preferentially binds to methylated linker DNA in the absence of the terminal tail of histone H3 and independently of histone acetylation
Author(s) -
Ishibashi Toyotaka,
Thambirajah Anita A.,
Ausió Juan
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.005
Subject(s) - linker dna , nucleosome , histone , linker , histone methylation , acetylation , chromatin , histone h3 , dna , biology , histone code , histone octamer , chemistry , microbiology and biotechnology , biochemistry , dna methylation , gene , gene expression , computer science , operating system
Methyl CpG binding protein 2 (MeCP2) is a basic protein that contains a DNA methyl binding domain. The mechanism by which the highly positive charge of MeCP2 and its ability to bind methylated DNA contribute to the specificity of its binding to chromatin has long remained elusive. In this paper, we show that MeCP2 binds to nucleosomes in a very similar way to linker histones both in vitro and in vivo . However, its binding specificity strongly depends on DNA methylation. We also observed that as with linker histones, this binding is independent of the core histone H3 N‐terminal tail and is not affected by histone acetylation.