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Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone.
Cho, Carol; Jang, Juwon; Kang, Yujin; Watanabe, Hiroki; Uchihashi, Takayuki; Kim, Seung Joong; Kato, Koichi; Lee, Ja Yil; Song, Ji-Joon.
Afiliación
  • Cho C; Department of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea. carol.cho@kaist.ac.kr.
  • Jang J; Department of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
  • Kang Y; School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan, Korea.
  • Watanabe H; Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Japan.
  • Uchihashi T; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan.
  • Kim SJ; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan.
  • Kato K; Department of Physics, Nagoya University, Nagoya, Japan.
  • Lee JY; Department of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
  • Song JJ; Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Japan.
Nat Commun ; 10(1): 5764, 2019 12 17.
Article en En | MEDLINE | ID: mdl-31848341
The fundamental unit of chromatin, the nucleosome, is an intricate structure that requires histone chaperones for assembly. ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, we demonstrate that the fission yeast ATAD2 homolog, Abo1, deposits histone H3-H4 onto DNA in an ATP-hydrolysis-dependent manner by in vitro reconstitution and single-tethered DNA curtain assays. We present cryo-EM structures of an ATAD2 family ATPase to atomic resolution in three different nucleotide states, revealing unique structural features required for histone loading on DNA, and directly visualize the transitions of Abo1 from an asymmetric spiral (ATP-state) to a symmetric ring (ADP- and apo-states) using high-speed atomic force microscopy (HS-AFM). Furthermore, we find that the acidic pore of ATP-Abo1 binds a peptide substrate which is suggestive of a histone tail. Based on these results, we propose a model whereby Abo1 facilitates H3-H4 loading by utilizing ATP.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Nucleosomas / Proteínas de Schizosaccharomyces pombe / Chaperonas de Histonas / ATPasas Asociadas con Actividades Celulares Diversas Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2019 Tipo del documento: Article Pais de publicación: Reino Unido
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Nucleosomas / Proteínas de Schizosaccharomyces pombe / Chaperonas de Histonas / ATPasas Asociadas con Actividades Celulares Diversas Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2019 Tipo del documento: Article Pais de publicación: Reino Unido