DNA damage response induces structural alterations in histone H3–H4

Synchrotron-radiation circular-dichroism spectroscopy was used to reveal that the DNA damage response induces a decrement of α-helix and an increment of β-strand contents of histone H3–H4 extracted from X-ray–irradiated human HeLa cells. The trend of the structural alteration was qualitatively oppos...

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Autores principales: Izumi, Yudai, Fujii, Kentaro, Yamamoto, Satoshi, Matsuo, Koichi, Namatame, Hirofumi, Taniguchi, Masaki, Yokoya, Akinari
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2017
Materias:
Regular Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5321191/
https://www.ncbi.nlm.nih.gov/pubmed/27672100
http://dx.doi.org/10.1093/jrr/rrw086
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author Izumi, Yudai
Fujii, Kentaro
Yamamoto, Satoshi
Matsuo, Koichi
Namatame, Hirofumi
Taniguchi, Masaki
Yokoya, Akinari
author_facet Izumi, Yudai
Fujii, Kentaro
Yamamoto, Satoshi
Matsuo, Koichi
Namatame, Hirofumi
Taniguchi, Masaki
Yokoya, Akinari
author_sort Izumi, Yudai
collection PubMed
description Synchrotron-radiation circular-dichroism spectroscopy was used to reveal that the DNA damage response induces a decrement of α-helix and an increment of β-strand contents of histone H3–H4 extracted from X-ray–irradiated human HeLa cells. The trend of the structural alteration was qualitatively opposite to that of our previously reported results for histone H2A–H2B. These results strongly suggest that histones share roles in DNA damage responses, particularly in DNA repair processes and chromatin remodeling, via a specific structural alteration of each histone.
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spelling pubmed-53211912017-02-27 DNA damage response induces structural alterations in histone H3–H4 Izumi, Yudai Fujii, Kentaro Yamamoto, Satoshi Matsuo, Koichi Namatame, Hirofumi Taniguchi, Masaki Yokoya, Akinari J Radiat Res Regular Paper Synchrotron-radiation circular-dichroism spectroscopy was used to reveal that the DNA damage response induces a decrement of α-helix and an increment of β-strand contents of histone H3–H4 extracted from X-ray–irradiated human HeLa cells. The trend of the structural alteration was qualitatively opposite to that of our previously reported results for histone H2A–H2B. These results strongly suggest that histones share roles in DNA damage responses, particularly in DNA repair processes and chromatin remodeling, via a specific structural alteration of each histone. Oxford University Press 2017-01 2017-01-23 /pmc/articles/PMC5321191/ /pubmed/27672100 http://dx.doi.org/10.1093/jrr/rrw086 Text en © The Author 2016. Published by Oxford University Press on behalf of The Japan Radiation Research Society and Japanese Society for Radiation Oncology. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Regular Paper
Izumi, Yudai
Fujii, Kentaro
Yamamoto, Satoshi
Matsuo, Koichi
Namatame, Hirofumi
Taniguchi, Masaki
Yokoya, Akinari
DNA damage response induces structural alterations in histone H3–H4
title DNA damage response induces structural alterations in histone H3–H4
title_full DNA damage response induces structural alterations in histone H3–H4
title_fullStr DNA damage response induces structural alterations in histone H3–H4
title_full_unstemmed DNA damage response induces structural alterations in histone H3–H4
title_short DNA damage response induces structural alterations in histone H3–H4
title_sort dna damage response induces structural alterations in histone h3–h4
topic Regular Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5321191/
https://www.ncbi.nlm.nih.gov/pubmed/27672100
http://dx.doi.org/10.1093/jrr/rrw086
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