ArticleMolecular and cellular biology1997
Nucleosome binding by the polymerase I transactivator upstream binding factor displaces linker histone H1.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 62 citations in OpenAlex.
- Regulation of RNA Polymerase I Stability and Function.Cancers · 2022Review
- Establishment and Maintenance of Open Ribosomal RNA Gene Chromatin States in Eukaryotes.Methods in molecular biology (Clifton, N.J.) · 2022Review
- A glitch in the snitch: the role of linker histone H1 in shaping the epigenome in normal and diseased cells.Open biology · 2021Review
- Review
- The missing linkGenes & development · 2021Review
- Review
- Ribosomal DNA and the nucleolus in the context of genome organization.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2019Review
- Differential hypomethylation of the repetitiveComparative cytogenetics · 2018Article
- PICH promotes mitotic chromosome segregation: Identification of a novel role in rDNA disjunction.Cell cycle (Georgetown, Tex.) · 2016Article
- Nucleolar organizer regions: genomic 'dark matter' requiring illumination.Genes & development · 2016Review
- Conditional inactivation of Upstream Binding Factor reveals its epigenetic functions and the existence of a somatic nucleolar precursor body.PLoS genetics · 2014Article
- Construction of synthetic nucleoli and what it tells us about propagation of sub-nuclear domains through cell division.Cell cycle (Georgetown, Tex.) · 2014Article
- TDP1 is an HMG chromatin protein facilitating RNA polymerase I transcription in African trypanosomes.Nucleic acids research · 2013Article
- Basic mechanisms in RNA polymerase I transcription of the ribosomal RNA genes.Sub-cellular biochemistry · 2013Review
- Identification of DHX33 as a mediator of rRNA synthesis and cell growth.Molecular and cellular biology · 2011Article
- Nucleolin is required for DNA methylation state and the expression of rRNA gene variants in Arabidopsis thaliana.PLoS genetics · 2010Article
- Regulation of nucleolar chromatin by B23/nucleophosmin jointly depends upon its RNA binding activity and transcription factor UBF.Molecular and cellular biology · 2010Article
- Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II.The Journal of cell biology · 2010Article
- Chromatin: linking structure and function in the nucleolus.Chromosoma · 2009Review
- UBF levels determine the number of active ribosomal RNA genes in mammals.The Journal of cell biology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Upstream binding factor (UBF) is a vertebrate RNA polymerase I transcription factor that can bend and wrap DNA. To investigate UBF's likely role as an architectural protein of rRNA genes organized in chromatin, we tested UBF's ability to bind rRNA gene enhancers assembled into nucleosome cores (DNA plus core histones) and nucleosomes (DNA plus core histones plus histone H1). UBF bound with low affinity to nucleosome cores formed with enhancer DNA probes of 162 bp. However, on nucleosome cores which contained approximately 60 bp of additional linker DNA, UBF bound with high affinity similar to its binding to naked DNA, forming a ternary DNA-core histone-UBF complex. UBF could be stripped from ternary complexes with competitor DNA to liberate nucleosome cores, rather than free DNA, suggesting that UBF binding to nucleosome cores does not displace the core histones H2A, H2B, H3, and H4. DNase I, micrococcal nuclease, and exonuclease III footprinting suggests that UBF and histone H1 interact with DNA on both sides flanking the histone octamer. Footprinting shows that UBF outcompetes histone H1 for binding to a nucleosome core and will displace, if not dissociate, H1 from its binding site on a preassembled nucleosome. These data suggest that UBF may act to prevent or reverse the assembly of transcriptionally inactive chromatin structures catalyzed by linker histone binding.
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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.