Summary information and primary citation
- PDB-id
-
9cau;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- cryo-EM (4.18 Å)
- Summary
- Deltaarp8 ino80 bound to s.c 0-40 nucleosome,
nucleosome
- Reference
-
Kaur U, Wu H, Cheng Y, Narlikar GJ (2025): "Autoinhibition
imposed by a large conformational switch of INO80
regulates nucleosome positioning." Science,
389, eadr3831. doi: 10.1126/science.adr3831.
- 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.
