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-Structure paper
Title | Structure and functional interactions of INO80 actin/Arp module. |
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Journal, issue, pages | J Mol Cell Biol, Vol. 11, Issue 5, Page 345-355, Year 2019 |
Publish date | May 1, 2019 |
Authors | Xuan Zhang / Xuejuan Wang / Zhihui Zhang / Gang Cai / |
PubMed 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. |
External links | J Mol Cell Biol / PubMed:30388237 / PubMed Central |
Methods | EM (single particle) |
Resolution | 13.1 - 28.201 Å |
Structure data | EMDB-6924: EMDB-9709: EMDB-9710: EMDB-9711: EMDB-9712: |
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