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TitleReorientation of INO80 on hexasomes reveals basis for mechanistic versatility.
Journal, issue, pagesScience, Vol. 381, Issue 6655, Page 319-324, Year 2023
Publish dateJul 21, 2023
AuthorsHao Wu / Elise N Muñoz / Laura J Hsieh / Un Seng Chio / Muryam A Gourdet / Geeta J Narlikar / Yifan Cheng /
PubMed AbstractUnlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report ...Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location -2 (SHL -2), in contrast to SHL -6 and SHL -7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL -2. The SHL -2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles.
External linksScience / PubMed:37384669 / PubMed Central
MethodsEM (single particle)
Resolution2.64 - 6.68 Å
Structure data

EMDB-28597, PDB-8ets:
Class1 of the INO80-Hexasome complex
Method: EM (single particle) / Resolution: 3.04 Å

EMDB-28598, PDB-8ett:
Class1 of the INO80-Hexasome complex
Method: EM (single particle) / Resolution: 6.68 Å

EMDB-28599, PDB-8etu:
Class2 of the INO80-Hexasome complex
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-28600, PDB-8etv:
Class2 of the INO80-Hexasome complex
Method: EM (single particle) / Resolution: 3.16 Å

EMDB-28601, PDB-8etw:
Class3 of INO80-Hexasome complex
Method: EM (single particle) / Resolution: 2.64 Å

EMDB-28602, PDB-8eu2:
Class3 of the INO80-Hexasome complex
Method: EM (single particle) / Resolution: 2.93 Å

EMDB-28609, PDB-8eu9:
Class1 of the INO80-Nucleosome complex
Method: EM (single particle) / Resolution: 3.48 Å

EMDB-28612, PDB-8eue:
Class1 of the INO80-Nucleosome complex
Method: EM (single particle) / Resolution: 3.48 Å

EMDB-28613, PDB-8euf:
Class2 of the INO80-Nucleosome complex
Method: EM (single particle) / Resolution: 3.41 Å

EMDB-28614, PDB-8euj:
Class2 of the INO80-Nucleosome complex
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • Baker's yeast (brewer's yeast)
  • xenopus laevis (African clawed frog)
  • synthetic construct (others)
  • xenopus (frog)
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsDNA BINDING PROTEIN / Chromatin Remodeler / hexasome / STRUCTURAL PROTEIN/DNA / STRUCTURAL PROTEIN-DNA complex / MOTOR PROTEIN/DNA / MOTOR PROTEIN-DNA complex / DNA BINDING PROTEIN/Hydrolase / DNA BINDING PROTEIN-Hydrolase complex / DNA BINDING PROTEIN/DNA / DNA BINDING PROTEIN-DNA complex

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