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-Structure paper
Title | Cryo-EM structures of the human INO80 chromatin-remodeling complex. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 25, Issue 1, Page 37-44, Year 2018 |
Publish date | Dec 4, 2017 |
Authors | Ricardo J Aramayo / Oliver Willhoft / Rafael Ayala / Rohan Bythell-Douglas / Dale B Wigley / Xiaodong Zhang / |
PubMed Abstract | Access to chromatin for processes such as transcription and DNA repair requires the sliding of nucleosomes along DNA. This process is aided by chromatin-remodeling complexes, such as the multisubunit ...Access to chromatin for processes such as transcription and DNA repair requires the sliding of nucleosomes along DNA. This process is aided by chromatin-remodeling complexes, such as the multisubunit INO80 chromatin-remodeling complex. Here we present cryo-EM structures of the active core complex of human INO80 at 9.6 Å, with portions at 4.1-Å resolution, and reconstructions of combinations of subunits. Together, these structures reveal the architecture of the INO80 complex, including Ino80 and actin-related proteins, which is assembled around a single RUVBL1 (Tip49a) and RUVBL2 (Tip49b) AAA+ heterohexamer. An unusual spoked-wheel structural domain of the Ino80 subunit is engulfed by this heterohexamer; both, in combination, form the core of the complex. We also identify a cleft in RUVBL1 and RUVBL2, which forms a major interaction site for partner proteins and probably communicates these interactions to its nucleotide-binding sites. |
External links | Nat Struct Mol Biol / PubMed:29323271 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.06 - 11.5 Å |
Structure data | EMDB-3772: EMDB-3773: High resolution INO80 core complex EMDB-3774: EMDB-3775: |
Chemicals | ChemComp-ADP: |
Source |
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Keywords | GENE REGULATION / Chromatin remodelling complex |