MeCP2 preferentially binds to methylated linker DNA in the absence of the terminal tail of histone H3 and independently of histone acetylation.
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.
Ishibashi
Toyotaka
T
Department of Biochemistry and Microbiology, The Center for Biomedical Research, University of Victoria, Victoria, BC, Canada V8W 3P6.
Thambirajah
Anita A
AA
Ausió
Juan
J
D000107:Acetylation; D001483:Base Sequence; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism*; D004247:DNA / Q000737:chemistry; D019175:DNA Methylation; D006367:HeLa Cells; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D051783:Methyl-CpG-Binding Protein 2 / Q000032:analysis / Q000378:metabolism*; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding
D002843:Chromatin; D006657:Histones; D051783:Methyl-CpG-Binding Protein 2; D009707:Nucleosomes; D004247:DNA