title: Physical methods used to study core histone tail structures and interactions in solution.
abstract: The core histone tail domains are key regulatory elements in chromatin. The tails are essential for folding oligonucleosomal arrays into both secondary and tertiary structures, and post-translational modifications within these domains can directly alter DNA accessibility. Unfortunately, there is little understanding of the structures and interactions of the core histone tail domains or how post-translational modifications within the tails may alter these interactions. Here we review NMR, thermal denaturation, cross-linking, and other selected solution methods used to define the general structures and binding behavior of the tail domains in various chromatin environments. All of these methods indicate that the tail domains bind primarily electrostatically to sites within chromatin. The data also indicate that the tails adopt specific structures when bound to DNA and that tail structures and interactions are plastic, depending on the specific chromatin environment. In addition, post-translational modifications, such as acetylation, can directly alter histone tail structures and interactions.
authors.affiliation: Department of Biochemistry and Biophysics, Box 712, University of Rochester Medical Center, 601 Elmwood Avenue, Rochester NY, USA.
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Wang
authors.forename: Jeffrey J
authors.initials: JJ
authors.lastname: Hayes
mesh_terms: D001665:Binding Sites; D003432:Cross-Linking Reagents; D004247:DNA / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009691:Nucleic Acid Denaturation; D011489:Protein Denaturation; D012996:Solutions; D011503:Transglutaminases / Q000378:metabolism
chemical_list: D003432:Cross-Linking Reagents; D006657:Histones; D012996:Solutions; D004247:DNA; D011503:Transglutaminases