Structural highlights
Function
H2A1_XENLA Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Publication Abstract from PubMed
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 A 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.
Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state.,Nodelman IM, Das S, Faustino AM, Fried SD, Bowman GD, Armache JP Nat Struct Mol Biol. 2022 Feb;29(2):121-129. doi: 10.1038/s41594-021-00719-x. , Epub 2022 Feb 16. PMID:35173352[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nodelman IM, Das S, Faustino AM, Fried SD, Bowman GD, Armache JP. Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state. Nat Struct Mol Biol. 2022 Feb;29(2):121-129. PMID:35173352 doi:10.1038/s41594-021-00719-x
