Regulated nucleosome mobility and the histone code.
Post-translational modifications of the histone tails are correlated with distinct chromatin states that regulate access to DNA. Recent proteomic analyses have revealed several new modifications in the globular nucleosome core, many of which lie at the histone-DNA interface. We interpret these modifications in light of previously published data and propose a new and testable model for how cells implement the histone code by modulating nucleosome dynamics.
Cosgrove
Michael S
MS
Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, 733 North Broadway Street, Baltimore, Maryland 21205, USA.
Boeke
Jef D
JD
Wolberger
Cynthia
C
D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D002843:Chromatin / Q000737:chemistry; D004247:DNA / Q000737:chemistry; D006657:Histones / Q000737:chemistry* / Q000502:physiology*; D006801:Humans; D006868:Hydrolysis; D008954:Models, Biological; D009707:Nucleosomes / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D000255:Adenosine Triphosphate; D004247:DNA