The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair

The complexity of chromatin architecture presents a significant barrier to the ability of the DNA repair machinery to access and repair DNA double-strand breaks (DSBs). Consequently, remodeling of the chromatin landscape adjacent to DSBs is vital for efficient DNA repair. Here, we demonstrate that D...

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Vydané v:	The Journal of cell biology Ročník 191; číslo 1; s. 31
Hlavní autori:	Xu, Ye, Sun, Yingli, Jiang, Xiaofeng, Ayrapetov, Marina K, Moskwa, Patryk, Yang, Shenghong, Weinstock, David M, Price, Brendan D
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 04.10.2010
Predmet:	Chromatin - metabolism Chromatin Assembly and Disassembly DNA Damage DNA Helicases - metabolism DNA Helicases - physiology DNA Repair DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology Histone Acetyltransferases - metabolism Histone Acetyltransferases - physiology Histones - metabolism Humans Lysine Acetyltransferase 5 Nucleosomes - metabolism Protein Stability Ubiquitination
ISSN:	1540-8140, 1540-8140
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Abstract	The complexity of chromatin architecture presents a significant barrier to the ability of the DNA repair machinery to access and repair DNA double-strand breaks (DSBs). Consequently, remodeling of the chromatin landscape adjacent to DSBs is vital for efficient DNA repair. Here, we demonstrate that DNA damage destabilizes nucleosomes within chromatin regions that correspond to the γ-H2AX domains surrounding DSBs. This nucleosome destabilization is an active process requiring the ATPase activity of the p400 SWI/SNF ATPase and histone acetylation by the Tip60 acetyltransferase. p400 is recruited to DSBs by a mechanism that is independent of ATM but requires mdc1. Further, the destabilization of nucleosomes by p400 is required for the RNF8-dependent ubiquitination of chromatin, and for the subsequent recruitment of brca1 and 53BP1 to DSBs. These results identify p400 as a novel DNA damage response protein and demonstrate that p400-mediated alterations in nucleosome and chromatin structure promote both chromatin ubiquitination and the accumulation of brca1 and 53BP1 at sites of DNA damage.
AbstractList	The complexity of chromatin architecture presents a significant barrier to the ability of the DNA repair machinery to access and repair DNA double-strand breaks (DSBs). Consequently, remodeling of the chromatin landscape adjacent to DSBs is vital for efficient DNA repair. Here, we demonstrate that DNA damage destabilizes nucleosomes within chromatin regions that correspond to the γ-H2AX domains surrounding DSBs. This nucleosome destabilization is an active process requiring the ATPase activity of the p400 SWI/SNF ATPase and histone acetylation by the Tip60 acetyltransferase. p400 is recruited to DSBs by a mechanism that is independent of ATM but requires mdc1. Further, the destabilization of nucleosomes by p400 is required for the RNF8-dependent ubiquitination of chromatin, and for the subsequent recruitment of brca1 and 53BP1 to DSBs. These results identify p400 as a novel DNA damage response protein and demonstrate that p400-mediated alterations in nucleosome and chromatin structure promote both chromatin ubiquitination and the accumulation of brca1 and 53BP1 at sites of DNA damage.The complexity of chromatin architecture presents a significant barrier to the ability of the DNA repair machinery to access and repair DNA double-strand breaks (DSBs). Consequently, remodeling of the chromatin landscape adjacent to DSBs is vital for efficient DNA repair. Here, we demonstrate that DNA damage destabilizes nucleosomes within chromatin regions that correspond to the γ-H2AX domains surrounding DSBs. This nucleosome destabilization is an active process requiring the ATPase activity of the p400 SWI/SNF ATPase and histone acetylation by the Tip60 acetyltransferase. p400 is recruited to DSBs by a mechanism that is independent of ATM but requires mdc1. Further, the destabilization of nucleosomes by p400 is required for the RNF8-dependent ubiquitination of chromatin, and for the subsequent recruitment of brca1 and 53BP1 to DSBs. These results identify p400 as a novel DNA damage response protein and demonstrate that p400-mediated alterations in nucleosome and chromatin structure promote both chromatin ubiquitination and the accumulation of brca1 and 53BP1 at sites of DNA damage. The complexity of chromatin architecture presents a significant barrier to the ability of the DNA repair machinery to access and repair DNA double-strand breaks (DSBs). Consequently, remodeling of the chromatin landscape adjacent to DSBs is vital for efficient DNA repair. Here, we demonstrate that DNA damage destabilizes nucleosomes within chromatin regions that correspond to the γ-H2AX domains surrounding DSBs. This nucleosome destabilization is an active process requiring the ATPase activity of the p400 SWI/SNF ATPase and histone acetylation by the Tip60 acetyltransferase. p400 is recruited to DSBs by a mechanism that is independent of ATM but requires mdc1. Further, the destabilization of nucleosomes by p400 is required for the RNF8-dependent ubiquitination of chromatin, and for the subsequent recruitment of brca1 and 53BP1 to DSBs. These results identify p400 as a novel DNA damage response protein and demonstrate that p400-mediated alterations in nucleosome and chromatin structure promote both chromatin ubiquitination and the accumulation of brca1 and 53BP1 at sites of DNA damage.
Author	Yang, Shenghong Xu, Ye Sun, Yingli Ayrapetov, Marina K Price, Brendan D Jiang, Xiaofeng Moskwa, Patryk Weinstock, David M
Author_xml	– sequence: 1 givenname: Ye surname: Xu fullname: Xu, Ye organization: Division of Genomic Stability and DNA Repair, Department of Radiation Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA – sequence: 2 givenname: Yingli surname: Sun fullname: Sun, Yingli – sequence: 3 givenname: Xiaofeng surname: Jiang fullname: Jiang, Xiaofeng – sequence: 4 givenname: Marina K surname: Ayrapetov fullname: Ayrapetov, Marina K – sequence: 5 givenname: Patryk surname: Moskwa fullname: Moskwa, Patryk – sequence: 6 givenname: Shenghong surname: Yang fullname: Yang, Shenghong – sequence: 7 givenname: David M surname: Weinstock fullname: Weinstock, David M – sequence: 8 givenname: Brendan D surname: Price fullname: Price, Brendan D
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/20876283$$D View this record in MEDLINE/PubMed
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Snippet	The complexity of chromatin architecture presents a significant barrier to the ability of the DNA repair machinery to access and repair DNA double-strand...
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StartPage	31
SubjectTerms	Chromatin - metabolism Chromatin Assembly and Disassembly DNA Damage DNA Helicases - metabolism DNA Helicases - physiology DNA Repair DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology Histone Acetyltransferases - metabolism Histone Acetyltransferases - physiology Histones - metabolism Humans Lysine Acetyltransferase 5 Nucleosomes - metabolism Protein Stability Ubiquitination
Title	The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair
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