EMD-17006

Single-particle
2.8 Å
EMD-17006 Deposition: 04/04/2023
Map released: 26/07/2023
Last modified: 24/07/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-17006

CryoEM Structure INO80core Hexasome complex composite map state1

EMD-17006

Single-particle
2.8 Å
EMD-17006 Deposition: 04/04/2023
Map released: 26/07/2023
Last modified: 24/07/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Thermochaetoides thermophila, Homo sapiens, synthetic construct
Sample: INO80 core module in complex with hexasome
Fitted models: 8oo7 (Avg. Q-score: 0.556)

Deposition Authors: Zhang M , Jungblut A , Hoffmann T , Eustermann S
Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling.
PUBMED: 37384673
DOI: doi:10.1126/science.adf6287
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of noncanonical nucleosomal particles remains largely elusive. In this work, we report the structural mechanism for adenosine 5'-triphosphate-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes noncanonical DNA and histone features of hexasomes that emerge from the loss of H2A-H2B. A large structural rearrangement 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.