Abstract

ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, authors find that the fission yeast ATAD2 homolog Abo1 deposits histone H3–H4 onto DNA in an ATP-hydrolysis-dependent manner, and present the cryo-EM structure of an ATAD2 family ATPase to reveal the structural basis of nucleosome assembly by Abo1.

Details

Title
Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone
Author
Cho, Carol 1 ; Jang, Juwon 1 ; Kang, Yujin 2 ; Watanabe, Hiroki 3   VIAFID ORCID Logo  ; Uchihashi, Takayuki 4   VIAFID ORCID Logo  ; Kim, Seung Joong 5 ; Kato, Koichi 6   VIAFID ORCID Logo  ; Lee, Ja Yil 2   VIAFID ORCID Logo  ; Ji-Joon Song 1   VIAFID ORCID Logo 

1  Department of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea 
2  School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan, Korea 
3  Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Japan; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan 
4  Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan; Department of Physics, Nagoya University, Nagoya, Japan 
5  Department of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea 
6  Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Japan; Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan; Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan 
Pages
1-13
Publication year
2019
Publication date
Dec 2019
Publisher
Nature Publishing Group
e-ISSN
20411723
Source type
Scholarly Journal
Language of publication
English
DOI
https://doi.org/10.1038/s41467-019-13743-9
ProQuest document ID
2327908913
Copyright
© 2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.