Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response

Yudai Izumi; Kentaro Fujii; Frank Wien; Chantal Houée-Lévin; Sandrine Lacombe; Daniela Salado-Leza; Erika Porcel; Rawand Masoud; Satoshi Yamamoto; Matthieu Réfrégiers; Marie-Anne Hervé du Penhoat; Akinari Yokoya

doi:10.1016/j.bpj.2016.06.002

Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response

Biophys J. 2016 Jul 12;111(1):69-78. doi: 10.1016/j.bpj.2016.06.002.

Affiliations

¹ Quantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan. Electronic address: izumi-yudai@hiroshima-u.ac.jp.
² Quantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan.
³ Synchrotron SOLEIL, Gif-sur-Yvette, France.
⁴ Laboratoire de Chimie Physique, CNRS UMR 8000, Université Paris Sud, Université Paris Saclay, Orsay, France.
⁵ Institut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
⁶ Graduate School of Science and Engineering, Ibaraki University, Ibaraki, Japan.
⁷ 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.
⁸ Quantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan; Graduate School of Science and Engineering, Ibaraki University, Ibaraki, Japan.

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.

MeSH terms

DNA Damage*
HeLa Cells
Histones / chemistry*
Histones / metabolism
Humans
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Temperature
Ubiquitination

Substances

Histones