ArticleThe Journal of biological chemistry2019
The Chd1 chromatin remodeler forms long-lived complexes with nucleosomes in the presence of ADP·BeF
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 7 citations in OpenAlex.
- Probing Centromere Plasticity and Chromatin Remodeling Using Single-Molecule Techniques.Cell biology international · 2026Review
- Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme.Science advances · 2026Article
- Molecular Acrobats: How CHD Remodelers Shape the Genetic Playground to License Cell Identity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026Article
- H2A.Z deposition by SWR1C involves multiple ATP-dependent steps.Nature communications · 2022Article
- SMARCAD1 is an ATP-dependent histone octamer exchange factor with de novo nucleosome assembly activity.Science advances · 2021Article
- Autoinhibitory elements of the Chd1 remodeler block initiation of twist defects by destabilizing the ATPase motor on the nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Architecture of the herpesvirus genome-packaging complex and implications for DNA translocation.Protein & cell · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Chromatin remodelers use helicase-like ATPase domains to reorganize histone-DNA contacts within the nucleosome. Like other remodelers, the chromodomain helicase DNA-binding protein 1 (Chd1) remodeler repositions nucleosomes by altering DNA topology at its internal binding site on the nucleosome, coupling different degrees of DNA twist and DNA movement to distinct nucleotide-bound states of the ATPase motor. In this work, we used a competition assay to study how variations in the bound nucleotide, Chd1, and the nucleosome substrate affect stability of Chd1-nucleosome complexes. We found that Chd1-nucleosome complexes formed in nucleotide-free or ADP conditions were relatively unstable and dissociated within 30 s, whereas those with the nonhydrolyzable ATP analog AMP-PNP had a mean lifetime of 4.8 ± 0.7 min. Chd1-nucleosome complexes were remarkably stable with ADP·BeF
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Registered trials
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