9GD1

Structure of Chd1 bound to a hexasome-nucleosome complex with a dyad-to-dyad distance of 103 bp.

This is a non-PDB format compatible entry.

Summary for 9GD1

• Entry DOI: 10.2210/pdb9gd1/pdb
• EMDB information: 51241
• Descriptor: Histone H3.2, MAGNESIUM ION, Histone H4, ... (10 entities in total)
• Functional Keywords: chromatin, remodeling, transcription, nucleosome, dna binding protein
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 17
• Total formula weight: 520824.96

Authors

Engeholm, M.,Roske, J.J.,Oberbeckmann, E.,Dienemann, C.,Lidschreiber, M.,Cramer, P.,Farnung, L. (deposition date: 2024-08-04, release date: 2024-09-18, Last modification date: 2024-10-02)

Primary citation

Engeholm, M.,Roske, J.J.,Oberbeckmann, E.,Dienemann, C.,Lidschreiber, M.,Cramer, P.,Farnung, L.
Resolution of transcription-induced hexasome-nucleosome complexes by Chd1 and FACT.
Mol.Cell, 84:3423-, 2024

PubMed Abstract: To maintain the nucleosome organization of transcribed genes, ATP-dependent chromatin remodelers collaborate with histone chaperones. Here, we show that at the 5' ends of yeast genes, RNA polymerase II (RNAPII) generates hexasomes that occur directly adjacent to nucleosomes. The resulting hexasome-nucleosome complexes are then resolved by Chd1. We present two cryoelectron microscopy (cryo-EM) structures of Chd1 bound to a hexasome-nucleosome complex before and after restoration of the missing inner H2A/H2B dimer by FACT. Chd1 uniquely interacts with the complex, positioning its ATPase domain to shift the hexasome away from the nucleosome. In the absence of the inner H2A/H2B dimer, its DNA-binding domain (DBD) packs against the ATPase domain, suggesting an inhibited state. Restoration of the dimer by FACT triggers a rearrangement that displaces the DBD and stimulates Chd1 remodeling. Our results demonstrate how chromatin remodelers interact with a complex nucleosome assembly and suggest how Chd1 and FACT jointly support transcription by RNAPII.

PubMed: 39270644
DOI: 10.1016/j.molcel.2024.08.022

Experimental method

ELECTRON MICROSCOPY (4 Å)