ArticleThe EMBO journal1998
Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
190 citing papers in PubMed, 1 synthesis or guideline pooled it, 391 citations in OpenAlex.
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- A genetic screen for regulators of Drosophila histone H1 binding and chromosome structure in vivo.Genetics · 2026Article
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- HIRA and dPCIF1 coordinately establish totipotent chromatin and control orderly ZGA inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Redirecting the pioneering function of FOXA1 with covalent small molecules.Molecular cell · 2024Article
- Characterization of Medusavirus encoded histones reveals nucleosome-like structures and a unique linker histone.Nature communications · 2024Article
- Genome access is transcription factor-specific and defined by nucleosome position.Molecular cell · 2024Article
130 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
The transcription factor HNF3 and linker histones H1 and H5 possess winged-helix DNA-binding domains, yet HNF3 and other fork head-related proteins activate genes during development whereas linker histones compact DNA in chromatin and repress gene expression. We compared how the two classes of factors interact with chromatin templates and found that HNF3 binds DNA at the side of nucleosome cores, similarly to what has been reported for linker histone. A nucleosome structural binding site for HNF3 is occupied at the albumin transcriptional enhancer in active and potentially active chromatin, but not in inactive chromatin in vivo. While wild-type HNF3 protein does not compact DNA extending from the nucleosome, as does linker histone, site-directed mutants of HNF3 can compact nucleosomal DNA if they contain basic amino acids at positions previously shown to be essential for nucleosomal DNA compaction by linker histones. The results illustrate how transcription factors can possess special nucleosome-binding activities that are not predicted from studies of factor interactions with free DNA.
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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.