EMD-28612
Class1 of the INO80-Nucleosome complex
EMD-28612
Single-particle3.48 Å
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Map released: 12/07/2023
Last modified: 03/04/2024
Sample Organism:
Xenopus,
synthetic construct
Sample: Class1 Nucleosome of the INO80-Nucleosome Complex
Fitted models: 8eue (Avg. Q-score: 0.356)
Deposition Authors: Wu H
,
Munoz E,
Gourdet M,
Narlikar G,
Cheng YF
Sample: Class1 Nucleosome of the INO80-Nucleosome Complex
Fitted models: 8eue (Avg. Q-score: 0.356)
Deposition Authors: Wu H
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Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility.
Wu H
,
Munoz EN
,
Hsieh LJ
,
Chio US
,
Gourdet MA
,
Narlikar GJ
,
Cheng Y
(2023) Science , 381 , 319 - 324
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(2023) Science , 381 , 319 - 324
Abstract:
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 Saccharomyces cerevisiae 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.
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 Saccharomyces cerevisiae 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.