Open AccessNucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state
Author(s) -
Ilana M. Nodelman,
Sayan Das,
Anneliese Faustino,
Stephen D. Fried,
Gregory D. Bowman,
Jean-Paul Armache
Publication year - 2022
Publication title -
nature structural and molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.448
H-Index - 270
eISSN - 1545-9993
pISSN - 1545-9985
DOI - 10.1038/s41594-021-00719-x
Subject(s) - nucleosome , chromatin , histone , dna , nucleotide , biophysics , biology , microbiology and biotechnology , chemistry , genetics , gene
Chromatin remodelers are ATP-dependent enzymes that reorganize nucleosomes within all eukaryotic genomes. Here we report a complex of the Chd1 remodeler bound to a nucleosome in a nucleotide-free state, determined by cryo-EM to 2.3 Å resolution. The remodeler stimulates the nucleosome to absorb an additional nucleotide on each strand at two different locations: on the tracking strand within the ATPase binding site and on the guide strand one helical turn from the ATPase motor. Remarkably, the additional nucleotide on the tracking strand is associated with a local transformation toward an A-form geometry, explaining how sequential ratcheting of each DNA strand occurs. The structure also reveals a histone-binding motif, ChEx, which can block opposing remodelers on the nucleosome and may allow Chd1 to participate in histone reorganization during transcription.