Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling
Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of non-canonical nucleosomal particles remains largely elusive. Here, we report the structural mechanism for ATP-dependent chromatin remodeling of hexasomes by the INO8...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2023-07, Vol.381 (6655), p.eadf6287-319 |
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| creator | Zhang, Min Jungblut, Anna Kunert, Franziska Hauptmann, Luis Hoffmann, Thomas Kolesnikova, Olga Metzner, Felix Moldt, Manuela Weis, Felix DiMaio, Frank Hopfner, Karl-Peter Eustermann, Sebastian |
| description | Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of non-canonical nucleosomal particles remains largely elusive. Here, we report the structural mechanism for ATP-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes non-canonical DNA and histone features of hexasomes emerging from the loss of H2A-H2B. A large structural re-arrangement switches the catalytic core of INO80 into a distinct, spin-rotated mode of remodeling, while its nuclear actin module remains tethered to long stretches of unwrapped linker DNA. Direct sensing of an exposed H3-H4 histone interface activates INO80, independently of the H2A-H2B acidic patch. Our findings reveal how the loss of H2A-H2B grants remodelers access to a different, yet unexplored, layer of energy-driven chromatin regulation. |
| doi_str_mv | 10.1126/science.adf6287 |
| format | Article |
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Here, we report the structural mechanism for ATP-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes non-canonical DNA and histone features of hexasomes emerging from the loss of H2A-H2B. A large structural re-arrangement switches the catalytic core of INO80 into a distinct, spin-rotated mode of remodeling, while its nuclear actin module remains tethered to long stretches of unwrapped linker DNA. Direct sensing of an exposed H3-H4 histone interface activates INO80, independently of the H2A-H2B acidic patch. 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| source | American Association for the Advancement of Science |
| subjects | Chromatin Deoxyribonucleic acid DNA Histones Nucleosomes Packaging Sliding |
| title | Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling |
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