Summary information and primary citation

PDB-id
8ooa; SNAP-derived features in text and JSON formats; DNAproDB
Class
DNA binding protein
Method
cryo-EM (3.18 Å)
Summary
Cryoem structure ino80core hexasome complex hexasome refinement state1
Reference
Zhang M, Jungblut A, Kunert F, Hauptmann L, Hoffmann T, Kolesnikova O, Metzner F, Moldt M, Weis F, DiMaio F, Hopfner KP, Eustermann S (2023): "Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling." Science, 381, 313-319. doi: 10.1126/science.adf6287.
Abstract
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js