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

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 t...

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Bibliographic Details
Published in:Biophysical journal 2016-07, Vol.111 (1), p.69-78
Main Authors: Izumi, Yudai, Fujii, Kentaro, Wien, Frank, Houée-Lévin, Chantal, Lacombe, Sandrine, Salado-Leza, Daniela, Porcel, Erika, Masoud, Rawand, Yamamoto, Satoshi, Réfrégiers, Matthieu, Hervé du Penhoat, Marie-Anne, Yokoya, Akinari
Format: Article
Language:English
Subjects:
DNA Damage
HeLa Cells
Histones - chemistry
Histones - metabolism
Humans
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Proteins
Temperature
Ubiquitination
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Summary: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.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2016.06.002