title: Histone variants--the structure behind the function.
abstract: In recent years, the chromatin field has witnessed a renewed interest in histone variants as pertaining to their structural role, but mainly because of the functional specificity they impart to chromatin. In this review, I am going to discuss several of the most recent structural studies on core histone (H2A.Bbd, H2A.Z, H2A.X, macroH2A, H3.3, CENP-A) and linker histone variants (histone H1 microheterogeneity) focusing on their role in nucleosome stability and chromatin fibre dynamics with special emphasis on their possible functional implications. The data accumulated to date indicates that histone variability plays an important role in the histone-mediated regulation of chromatin metabolism. Understanding and deciphering the underlying structural amino acid code behind such variability remains one of the most exciting future challenges in chromatin research.
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada. jausio@uvic.ca
authors.forename: Juan
authors.initials: J
authors.lastname: Ausió
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D016415:Sequence Alignment
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes