title: Comparison between the CENP-A and histone H3 structures in nucleosomes.
abstract: Centromeres are epigenetically marked by the assembly of nucleosomes containing the centromere-specific histone H3 variant, CENP-A (CENP-A nucleosome) and their inheritance is probably dictated by the architecture of the centromeric nucleosome. We previously determined the crystal structure of the human CENP-A nucleosome. CENP-A forms a histone octamer containing two each of histones H2A, H2B, H4 and CENP-A and the DNA is left-handedly wrapped around the histone octamer, as in canonical nucleosomes containing histone H3. In the CENP-A nucleosome structure, 13 base pairs of the DNA ends are detached from the histone surface and two CENP-A regions, the αN helix and loop 1, adopt different structures from those in the H3 nucleosome. In this Extra View article, we provide a detailed structural comparison between CENP-A and H3 in nucleosomes and describe their distinctions and similarities.
authors: Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
authors: Hiroaki
authors: H
authors: Tachiwana
authors: Wataru
authors: W
authors: Kagawa
authors: Hitoshi
authors: H
authors: Kurumizaka
mesh_terms: D001324:Autoantigens / Q000737:chemistry* / Q000378:metabolism; D000076247:Centromere Protein A; D051936:Centromere Protein B / Q000737:chemistry / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D001324:Autoantigens; C000619700:CENPA protein, human; D000076247:Centromere Protein A; D051936:Centromere Protein B; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D009707:Nucleosomes; D004247:DNA