DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.

Actin and actin-related proteins (Arps), which are members of the actin family, are essential components of many of these remodeling complexes. Actin, Arp4, Arp5, and Arp8 are found to be evolutionarily conserved components of the INO80 chromatin remodeling complex, which is involved in transcriptio...

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Autores principales:	Akihisa Osakabe, Yuichiro Takahashi, Hirokazu Murakami, Kenji Otawa, Hiroaki Tachiwana, Yukako Oma, Hitoshi Nishijima, Kei-ich Shibahara, Hitoshi Kurumizaka, Masahiko Harata
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ebbb0ae720fd44b98e714bedae0b0269
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spelling	oai:doaj.org-article:ebbb0ae720fd44b98e714bedae0b02692021-11-25T05:57:15ZDNA binding properties of the actin-related protein Arp8 and its role in DNA repair.1932-620310.1371/journal.pone.0108354https://doaj.org/article/ebbb0ae720fd44b98e714bedae0b02692014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0108354https://doaj.org/toc/1932-6203Actin and actin-related proteins (Arps), which are members of the actin family, are essential components of many of these remodeling complexes. Actin, Arp4, Arp5, and Arp8 are found to be evolutionarily conserved components of the INO80 chromatin remodeling complex, which is involved in transcriptional regulation, DNA replication, and DNA repair. A recent report showed that Arp8 forms a module in the INO80 complex and this module can directly capture a nucleosome. In the present study, we showed that recombinant human Arp8 binds to DNAs, and preferentially binds to single-stranded DNA. Analysis of the binding of adenine nucleotides to Arp8 mutants suggested that the ATP-binding pocket, located in the evolutionarily conserved actin fold, plays a regulatory role in the binding of Arp8 to DNA. To determine the cellular function of Arp8, we derived tetracycline-inducible Arp8 knockout cells from a cultured human cell line. Analysis of results obtained after treating these cells with aphidicolin and camptothecin revealed that Arp8 is involved in DNA repair. Together with the previous observation that Arp8, but not γ-H2AX, is indispensable for recruiting INO80 complex to DSB in human, results of our study suggest an individual role for Arp8 in DNA repair.Akihisa OsakabeYuichiro TakahashiHirokazu MurakamiKenji OtawaHiroaki TachiwanaYukako OmaHitoshi NishijimaKei-ich ShibaharaHitoshi KurumizakaMasahiko HarataPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 10, p e108354 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Akihisa Osakabe Yuichiro Takahashi Hirokazu Murakami Kenji Otawa Hiroaki Tachiwana Yukako Oma Hitoshi Nishijima Kei-ich Shibahara Hitoshi Kurumizaka Masahiko Harata DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.
description	Actin and actin-related proteins (Arps), which are members of the actin family, are essential components of many of these remodeling complexes. Actin, Arp4, Arp5, and Arp8 are found to be evolutionarily conserved components of the INO80 chromatin remodeling complex, which is involved in transcriptional regulation, DNA replication, and DNA repair. A recent report showed that Arp8 forms a module in the INO80 complex and this module can directly capture a nucleosome. In the present study, we showed that recombinant human Arp8 binds to DNAs, and preferentially binds to single-stranded DNA. Analysis of the binding of adenine nucleotides to Arp8 mutants suggested that the ATP-binding pocket, located in the evolutionarily conserved actin fold, plays a regulatory role in the binding of Arp8 to DNA. To determine the cellular function of Arp8, we derived tetracycline-inducible Arp8 knockout cells from a cultured human cell line. Analysis of results obtained after treating these cells with aphidicolin and camptothecin revealed that Arp8 is involved in DNA repair. Together with the previous observation that Arp8, but not γ-H2AX, is indispensable for recruiting INO80 complex to DSB in human, results of our study suggest an individual role for Arp8 in DNA repair.
format	article
author	Akihisa Osakabe Yuichiro Takahashi Hirokazu Murakami Kenji Otawa Hiroaki Tachiwana Yukako Oma Hitoshi Nishijima Kei-ich Shibahara Hitoshi Kurumizaka Masahiko Harata
author_facet	Akihisa Osakabe Yuichiro Takahashi Hirokazu Murakami Kenji Otawa Hiroaki Tachiwana Yukako Oma Hitoshi Nishijima Kei-ich Shibahara Hitoshi Kurumizaka Masahiko Harata
author_sort	Akihisa Osakabe
title	DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.
title_short	DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.
title_full	DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.
title_fullStr	DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.
title_full_unstemmed	DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.
title_sort	dna binding properties of the actin-related protein arp8 and its role in dna repair.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/ebbb0ae720fd44b98e714bedae0b0269
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DNA binding properties of the actin-related protein Arp8 and its role in DNA repair.

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