ArticleNature2009
The chromatin remodeller ACF acts as a dimeric motor to space nucleosomes.
Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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Who cites it
112 citing papers in PubMed, 178 citations in OpenAlex.
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- Identification of compounds that repress DUX4 expression in facioscapulohumeral muscular dystrophy.bioRxiv : the preprint server for biology · 2026Article
- Bromodomain-Driven Regulation of Stem Cells: A Potential Target for Cancer Therapeutic Intervention.Stem cell reviews and reports · 2026Review
- Spatiotemporal control of SMARCA5 by a MAPK-RUNX1 axis distinguishes mutant KRAS-driven pancreatic malignancy from tissue regeneration.Nature cancer · 2026Article
- Distinct transcriptomic signatures in pulmonary tissue resident and vascular resident-like T cells in nonhuman primates.iScience · 2025Article
- Alternative splicing of BAZ1A in colorectal cancer disrupts the DNA damage response and increases chemosensitization.Cell death & disease · 2024Article
- Structures of H2A.Z-associated human chromatin remodelers SRCAP and TIP60 reveal divergent mechanisms of chromatin engagement.bioRxiv : the preprint server for biology · 2024Article
- Chromatin remodelers: a concise introduction for biophysicists.Biophysical reviews · 2024Review
- Energy-driven genome regulation by ATP-dependent chromatin remodellers.Nature reviews. Molecular cell biology · 2024Review
- Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking.Nature communications · 2024Article
- Nucleosome density shapes kilobase-scale regulation by a mammalian chromatin remodeler.Nature structural & molecular biology · 2023Article
- ATP Hydrolysis Coordinates the Activities of Two Motors in a Dimeric Chromatin Remodeling Enzyme.Journal of molecular biology · 2022Article
- Acetylation-dependent SAGA complex dimerization promotes nucleosome acetylation and gene transcription.Nature structural & molecular biology · 2022Article
- Astaxanthin Attenuates the Changes in the Expression of MicroRNAs Involved in the Activation of Hepatic Stellate Cells.Nutrients · 2022Article
- Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state.Nature structural & molecular biology · 2022Article
- How to Kinetically Dissect an RNA Machine.Biochemistry · 2021Article
- Collaboration through chromatin: motors of transcription and chromatin structure.Journal of molecular biology · 2021Review
- Sophisticated Conversations between Chromatin and Chromatin Remodelers, and Dissonances in Cancer.International journal of molecular sciences · 2021Review
- Genome-wide chromatin occupancy of BRDT and gene expression analysis suggest transcriptional partners and specific epigenetic landscapes that regulate gene expression during spermatogenesis.Molecular reproduction and development · 2021Article
52 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Evenly spaced nucleosomes directly correlate with condensed chromatin and gene silencing. The ATP-dependent chromatin assembly factor (ACF) forms such structures in vitro and is required for silencing in vivo. ACF generates and maintains nucleosome spacing by constantly moving a nucleosome towards the longer flanking DNA faster than the shorter flanking DNA. How the enzyme rapidly moves back and forth between both sides of a nucleosome to accomplish bidirectional movement is unknown. Here we show that nucleosome movement depends cooperatively on two ACF molecules, indicating that ACF functions as a dimer of ATPases. Further, the nucleotide state determines whether the dimer closely engages one or both sides of the nucleosome. Three-dimensional reconstruction by single-particle electron microscopy of the ATPase-nucleosome complex in an activated ATP state reveals a dimer architecture in which the two ATPases face each other. Our results indicate a model in which the two ATPases work in a coordinated manner, taking turns to engage either side of a nucleosome, thereby allowing processive bidirectional movement. This novel dimeric motor mechanism differs from that of dimeric motors such as kinesin and dimeric helicases that processively translocate unidirectionally and reflects the unique challenges faced by motors that move nucleosomes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.