9C9G

S.c INO80 in complex with S.c 0/80 nucleosome

This is a non-PDB format compatible entry.

Summary for 9C9G

• Entry DOI: 10.2210/pdb9c9g/pdb
• EMDB information: 45361
• Descriptor: Histone H3, Histone H4, DNA (227-MER), ... (13 entities in total)
• Functional Keywords: chromatin remodeler, nucleosome, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Saccharomyces cerevisiae (brewer's yeast); More
• Total number of polymer chains: 20
• Total formula weight: 873632.67

Authors

Wu, H.,Kaur, U.,Narlikar, G.J.,Cheng, Y.F. (deposition date: 2024-06-13, release date: 2025-07-16, Last modification date: 2025-07-30)

Primary citation

Kaur, U.,Wu, H.,Cheng, Y.,Narlikar, G.J.
Autoinhibition imposed by a large conformational switch of INO80 regulates nucleosome positioning.
Science, 389:eadr3831-eadr3831, 2025

PubMed Abstract: Increasing the flanking DNA from 40 to 80 base pairs (bp) causes ~100-fold faster nucleosome sliding by INO80. A prevalent hypothesis posits that the Arp8 module within INO80 enables a ruler-like activity. Using cryogenic electron microscopy, we show that on nucleosomes with 40 bp of flanking DNA, the Arp8 module rotates 180° away from the DNA. Deleting the Arp8 module enables rapid sliding irrespective of flanking DNA length. Thus, rather than enabling a ruler-like activity, the Arp8 module acts as a brake on INO80 remodeling when flanking DNA is short. This autoinhibition-based mechanism has broad implications for understanding how primitive nucleosome mobilization enzymes may have evolved into sophisticated remodelers.

PubMed: 40674492
DOI: 10.1126/science.adr3831

Experimental method

ELECTRON MICROSCOPY (2.91 Å)