Ministry of Science and Technology of the People Republic of China
2014CB910700
China
Citation
Journal: J Mol Cell Biol / Year: 2019 Title: Structure and functional interactions of INO80 actin/Arp module. Authors: Xuan Zhang / Xuejuan Wang / Zhihui Zhang / Gang Cai / 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 ...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.
History
Deposition
Feb 28, 2018
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Header (metadata) release
Dec 12, 2018
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Map release
Dec 12, 2018
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Update
Jun 26, 2019
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Current status
Jun 26, 2019
Processing site: PDBj / Status: Released
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