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DDB2 promotes chromatin decondensation at UV-induced DNA damage
Nucleotide excision repair (NER) is the principal pathway that removes helix-distorting deoxyribonucleic acid (DNA) damage from the mammalian genome. Recognition of DNA lesions by xeroderma pigmentosum group C (XPC) protein in chromatin is stimulated by the damaged DNA-binding protein 2 (DDB2), whic...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3328393/ https://www.ncbi.nlm.nih.gov/pubmed/22492724 http://dx.doi.org/10.1083/jcb.201106074 |
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author | Luijsterburg, Martijn S. Lindh, Michael Acs, Klara Vrouwe, Mischa G. Pines, Alex van Attikum, Haico Mullenders, Leon H. Dantuma, Nico P. |
author_facet | Luijsterburg, Martijn S. Lindh, Michael Acs, Klara Vrouwe, Mischa G. Pines, Alex van Attikum, Haico Mullenders, Leon H. Dantuma, Nico P. |
author_sort | Luijsterburg, Martijn S. |
collection | PubMed |
description | Nucleotide excision repair (NER) is the principal pathway that removes helix-distorting deoxyribonucleic acid (DNA) damage from the mammalian genome. Recognition of DNA lesions by xeroderma pigmentosum group C (XPC) protein in chromatin is stimulated by the damaged DNA-binding protein 2 (DDB2), which is part of a CUL4A–RING ubiquitin ligase (CRL4) complex. In this paper, we report a new function of DDB2 in modulating chromatin structure at DNA lesions. We show that DDB2 elicits unfolding of large-scale chromatin structure independently of the CRL4 ubiquitin ligase complex. Our data reveal a marked adenosine triphosphate (ATP)–dependent reduction in the density of core histones in chromatin containing UV-induced DNA lesions, which strictly required functional DDB2 and involved the activity of poly(adenosine diphosphate [ADP]–ribose) polymerase 1. Finally, we show that lesion recognition by XPC, but not DDB2, was strongly reduced in ATP-depleted cells and was regulated by the steady-state levels of poly(ADP-ribose) chains. |
format | Online Article Text |
id | pubmed-3328393 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-33283932012-10-16 DDB2 promotes chromatin decondensation at UV-induced DNA damage Luijsterburg, Martijn S. Lindh, Michael Acs, Klara Vrouwe, Mischa G. Pines, Alex van Attikum, Haico Mullenders, Leon H. Dantuma, Nico P. J Cell Biol Research Articles Nucleotide excision repair (NER) is the principal pathway that removes helix-distorting deoxyribonucleic acid (DNA) damage from the mammalian genome. Recognition of DNA lesions by xeroderma pigmentosum group C (XPC) protein in chromatin is stimulated by the damaged DNA-binding protein 2 (DDB2), which is part of a CUL4A–RING ubiquitin ligase (CRL4) complex. In this paper, we report a new function of DDB2 in modulating chromatin structure at DNA lesions. We show that DDB2 elicits unfolding of large-scale chromatin structure independently of the CRL4 ubiquitin ligase complex. Our data reveal a marked adenosine triphosphate (ATP)–dependent reduction in the density of core histones in chromatin containing UV-induced DNA lesions, which strictly required functional DDB2 and involved the activity of poly(adenosine diphosphate [ADP]–ribose) polymerase 1. Finally, we show that lesion recognition by XPC, but not DDB2, was strongly reduced in ATP-depleted cells and was regulated by the steady-state levels of poly(ADP-ribose) chains. The Rockefeller University Press 2012-04-16 /pmc/articles/PMC3328393/ /pubmed/22492724 http://dx.doi.org/10.1083/jcb.201106074 Text en © 2012 Luijsterburg et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Luijsterburg, Martijn S. Lindh, Michael Acs, Klara Vrouwe, Mischa G. Pines, Alex van Attikum, Haico Mullenders, Leon H. Dantuma, Nico P. DDB2 promotes chromatin decondensation at UV-induced DNA damage |
title | DDB2 promotes chromatin decondensation at UV-induced DNA damage |
title_full | DDB2 promotes chromatin decondensation at UV-induced DNA damage |
title_fullStr | DDB2 promotes chromatin decondensation at UV-induced DNA damage |
title_full_unstemmed | DDB2 promotes chromatin decondensation at UV-induced DNA damage |
title_short | DDB2 promotes chromatin decondensation at UV-induced DNA damage |
title_sort | ddb2 promotes chromatin decondensation at uv-induced dna damage |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3328393/ https://www.ncbi.nlm.nih.gov/pubmed/22492724 http://dx.doi.org/10.1083/jcb.201106074 |
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