ArticleBiochimica et biophysica acta. General subjects2021
Transcription factor NF-κB unravels nucleosomes.
Article in Biochimica et biophysica acta. General subjects, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Analysis of DNA-Protein Complexes by Atomic Force Microscopy Imaging: The Case of TRF2-Telomeric DNA Wrapping.Methods in molecular biology (Clifton, N.J.) · 2027Article
- The Causal Role of Bile Acids in Cancers of the Digestive System.Biomedicines · 2026Review
- Transposon invasion of primate genomes shaped human inflammatory enhancers and susceptibility to inflammatory diseases.Nature communications · 2025Article
- Time-varying stimuli that prolong IKK activation promote nuclear remodeling and mechanistic switching of NF-κB dynamics.Nature communications · 2025Article
- The Role of Lactylation in Virus-Host Interactions.International journal of molecular sciences · 2025Review
- Nanoscale Characterization of Interaction of Nucleosomes with H1 Linker Histone.International journal of molecular sciences · 2024Article
- The Interaction of NF-κB Transcription Factor with Centromeric Chromatin.The journal of physical chemistry. B · 2024Article
- The transcription factor NF-κB orchestrates nucleosome remodeling during the primary response to Toll-like receptor 4 signaling.Immunity · 2024Article
- Three-Way DNA Junction as an End Label for DNA in Atomic Force Microscopy Studies.International journal of molecular sciences · 2022Article
- The Sequence Dependent Nanoscale Structure of CENP-A Nucleosomes.International journal of molecular sciences · 2022Article
- Structures and consequences of pioneer factor binding to nucleosomes.Current opinion in structural biology · 2022Review
- Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
NF-κB is a transcription factor responsible for activating hundreds of genes in mammalian organisms. To accomplish its function, NF-κB must interact with DNA occupied by nucleosomes, but how this interaction occurs is unclear. Here we used Atomic Force Microscopy to characterize complexes of NF-κB with nucleosomes assembled on different DNA templates. The assembly of NF-κB-nucleosome complexes leads to a substantial decrease of DNA wrapping efficiency from 149 ± 2 bp (SEM) for the control nucleosome sample to 135 ± 3 bp for complexes of nucleosomes with NF-κB. Mapping of the nucleosomes did not reveal displacement of under-wrapped nucleosomes from their original position, suggesting that unravelling involves dissociation of one or both flanks of the nucleosomes. Binding of NF-κB to the core was identified by nucleosome core volume measurements. We discovered two binding modes of NF-κB associated with nucleosome unravelling - NF-κB bound to the nucleosome core and to the DNA flanks. From these findings we propose two models explaining the interaction of NF-κB with the nucleosome complex. The partial unravelling of nucleosomes by NF-κB makes the DNA segment at the edge of the nucleosome core accessible, facilitating the transcription process. We speculate that NF-κB can function as a pioneer factor, enhancing its ability to facilitate rapid transcriptional response to cell stress.
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