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Structure and functional interactions of INO80 actin/Arp module.

Authors
  • Zhang, Xuan1
  • Wang, Xuejuan1
  • Zhang, Zhihui1
  • Cai, Gang1, 2
  • 1 Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei, China. , (China)
  • 2 CAS Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Hefei, China. , (China)
Type
Published Article
Journal
Journal of molecular cell biology
Publication Date
May 01, 2019
Volume
11
Issue
5
Pages
345–355
Identifiers
DOI: 10.1093/jmcb/mjy062
PMID: 30388237
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The presence and functions of nuclear actin have been controversial due to the lack of molecular mechanisms. Nuclear actin and actin-related proteins (Arps) are subunits of several chromatin remodelers, including the evolutionarily conserved INO80 chromatin-remodeling complex. Here, we present an improved cryo-EM structure of the yeast INO80 complex and the first 3D reconstruction of the INO80 actin/Arp module. The modular and subunit architecture is defined using a combination of subunit deletion analysis and published crosslinking-mass spectrometry. The functional interactions of the INO80 actin/Arp module with a nucleosome is 3D EM reconstructed in two different binding states. Nucleosomes initially bind to the Arp8 subunit and the substantial conformational changes maximize nucleosome contacts of the actin/Arp module, which could promote the bound nucleosome to be engaged onto the INO80 ATPase domain. Our findings suggest that the conserved nuclear actin/Arp module acts a conformational switch of the INO80 for nucleosome binding. © The Author(s) (2018). Published by Oxford University Press on behalf of Journal of Molecular Cell Biology, IBCB, SIBS, CAS.

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