title: Histone structure and nucleosome stability.
abstract: Histone proteins play essential structural and functional roles in the transition between active and inactive chromatin states. Although histones have a high degree of conservation due to constraints to maintain the overall structure of the nucleosomal octameric core, variants have evolved to assume diverse roles in gene regulation and epigenetic silencing. Histone variants, post-translational modifications and interactions with chromatin remodeling complexes influence DNA replication, transcription, repair and recombination. The authors review recent findings on the structure of chromatin that confirm previous interparticle interactions observed in crystal structures.
authors.affiliation: Computational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA. marino@ncbi.nlm.nih.gov
authors.forename: Leonardo
authors.initials: L
authors.lastname: Mariño-Ramírez
authors.forename: Maricel G
authors.initials: MG
authors.lastname: Kann
authors.forename: Benjamin A
authors.initials: BA
authors.lastname: Shoemaker
authors.forename: David
authors.initials: D
authors.lastname: Landsman
mesh_terms: D000818:Animals; D042002:Chromatin Assembly and Disassembly; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000235:genetics
chemical_list: D006657:Histones; D009707:Nucleosomes