title: H1 and HMGB1: modulators of chromatin structure.
abstract: Histone H1 and HMGB1 (high-mobility group protein B1) are the most abundant chromosomal proteins apart from the core histones (on average, one copy per nucleosome and per ten nucleosomes respectively). They are both highly mobile in the cell nucleus, with high on/off rates for binding. In vivo and in vitro evidence shows that both are able to organize chromatin structure, with H1 binding resulting in a more stable structure and HMGB1 binding in a less stable structure. The binding sites for H1 and HMGB1 in chromatin are partially overlapping, and replacement of H1 by HMGB1 through the highly dynamic nature of their binding, possibly facilitated by interaction between them, could result in switching of chromatin states. Binding of HMGB1 to DNA or chromatin is regulated by its long and highly acidic tail, which is also involved in H1 binding. The present article focuses mainly on HMGB1 and its interaction with chromatin and H1, as well as its chaperone role in the binding of certain transcription factors (e.g. p53) to their cognate DNA.
authors.affiliation: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, U.K. jot1@cam.ac.uk
authors.forename: Jean O
authors.initials: JO
authors.lastname: Thomas
authors.forename: Katherine
authors.initials: K
authors.lastname: Stott
mesh_terms: D000818:Animals; D002843:Chromatin / Q000737:chemistry* / Q000378:metabolism*; D024243:HMGB1 Protein / Q000737:chemistry / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D011485:Protein Binding
chemical_list: D002843:Chromatin; D024243:HMGB1 Protein; D006657:Histones; D018832:Molecular Chaperones