8OOK

CryoEM Structure INO80core Hexasome complex Arp5 grappler refinement state1

Summary for 8OOK

• Entry DOI: 10.2210/pdb8ook/pdb
• EMDB information: 17006 17017 17019
• Descriptor: Actin-related protein 5 (1 entity in total)
• Functional Keywords: atp-dependent chromatin remodeler, dna binding protein
• Biological source: Thermochaetoides thermophila
• Total number of polymer chains: 1
• Total formula weight: 87773.09

Authors

Zhang, M.,Jungblut, A.,Hoffmann, T.,Eustermann, S. (deposition date: 2023-04-05, release date: 2023-07-26, Last modification date: 2024-07-24)

Primary citation

Zhang, M.,Jungblut, A.,Kunert, F.,Hauptmann, L.,Hoffmann, T.,Kolesnikova, O.,Metzner, F.,Moldt, M.,Weis, F.,DiMaio, F.,Hopfner, K.P.,Eustermann, S.
Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling.
Science, 381:313-319, 2023

PubMed 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.

PubMed: 37384673
DOI: 10.1126/science.adf6287

Experimental method

ELECTRON MICROSCOPY (5.69 Å)