title: Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response.
abstract: Using synchrotron radiation-based circular dichroism spectroscopy, we found that the DNA damage response induces an increase of α-helix structure and a decrease of β-strand and turn structures in histone H2A-H2B extracted from x-irradiated human HeLa cells. The structural alterations correspond to the assumption that an average of eight amino acid residues form new α-helix structures at 310 K. We propose the structural transition from β-strand and turn structures to an α-helix structure in H2A-H2B as a novel, to our knowledge, process involved in the DNA damage response.
authors.affiliation: Quantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan. Electronic address: izumi-yudai@hiroshima-u.ac.jp.
authors.forename: Yudai
authors.initials: Y
authors.lastname: Izumi
authors.affiliation: Quantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan.
authors.forename: Kentaro
authors.initials: K
authors.lastname: Fujii
authors.affiliation: Synchrotron SOLEIL, Gif-sur-Yvette, France.
authors.forename: Frank
authors.initials: F
authors.lastname: Wien
authors.affiliation: Laboratoire de Chimie Physique, CNRS UMR 8000, Université Paris Sud, Université Paris Saclay, Orsay, France.
authors.forename: Chantal
authors.initials: C
authors.lastname: Houée-Lévin
authors.affiliation: Institut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
authors.forename: Sandrine
authors.initials: S
authors.lastname: Lacombe
authors.affiliation: Institut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
authors.forename: Daniela
authors.initials: D
authors.lastname: Salado-Leza
authors.affiliation: Institut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
authors.forename: Erika
authors.initials: E
authors.lastname: Porcel
authors.affiliation: Laboratoire de Chimie Physique, CNRS UMR 8000, Université Paris Sud, Université Paris Saclay, Orsay, France.
authors.forename: Rawand
authors.initials: R
authors.lastname: Masoud
authors.affiliation: Graduate School of Science and Engineering, Ibaraki University, Ibaraki, Japan.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Yamamoto
authors.affiliation: Synchrotron SOLEIL, Gif-sur-Yvette, France.
authors.forename: Matthieu
authors.initials: M
authors.lastname: Réfrégiers
authors.affiliation: Institut de Minéralogie, de Physique des Matériaux, et de Cosmochimie, Sorbonne Universités-UPMC Univ Paris 06, UMR CNRS 7590, MNHN, IRD UMR 206, Paris, France.
authors.forename: Marie-Anne
authors.initials: MA
authors.lastname: Hervé du Penhoat
authors.affiliation: Quantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan; Graduate School of Science and Engineering, Ibaraki University, Ibaraki, Japan.
authors.forename: Akinari
authors.initials: A
authors.lastname: Yokoya
mesh_terms: D004249:DNA Damage; D006367:HeLa Cells; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D013696:Temperature; D054875:Ubiquitination
chemical_list: D006657:Histones