ArticleNature communications2022
Structural basis of RNA polymerase II transcription on the chromatosome containing linker histone H1.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Structural basis of RNA polymerase II transcription on the histone H3-H4 octasome.The Journal of biological chemistry · 2026Article
- REST elevation-dependent chromatin remodeling and alternative Grk6 transcript synthesis hyperactivates Cxcr4-Sdf1 signaling in cerebellar granule cell progenitors.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into how DEK nucleosome binding facilitates H3K27 trimethylation in chromatin.Nature structural & molecular biology · 2025Article
- Structural insights into promoter-proximal pausing of RNA polymerase II at +1 nucleosome.Science advances · 2025Article
- RNA Polymerase II Activity Control of Gene Expression and Involvement in Disease.Journal of molecular biology · 2025Review
- Linker histones enhance robustness in diurnal transcription dynamics.Quantitative plant biology · 2025Article
- A Site-Specific Click Chemistry Approach to Di-Ubiquitylate H1 Variants Reveals Position-Dependent Stimulation of the DNA Repair Protein RNF168.Angewandte Chemie (International ed. in English) · 2024Article
- Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2.Nucleic acids research · 2024Article
- The Nucleic Acid Knowledgebase: a new portal for 3D structural information about nucleic acids.Nucleic acids research · 2024Article
- Collaborators or competitors: the communication between RNA polymerase II and the nucleosome during eukaryotic transcription.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In chromatin, linker histone H1 binds to nucleosomes, forming chromatosomes, and changes the transcription status. However, the mechanism by which RNA polymerase II (RNAPII) transcribes the DNA in the chromatosome has remained enigmatic. Here we report the cryo-electron microscopy (cryo-EM) structures of transcribing RNAPII-chromatosome complexes (forms I and II), in which RNAPII is paused at the entry linker DNA region of the chromatosome due to H1 binding. In the form I complex, the H1 bound to the nucleosome restricts the linker DNA orientation, and the exit linker DNA is captured by the RNAPII DNA binding cleft. In the form II complex, the RNAPII progresses a few bases ahead by releasing the exit linker DNA from the RNAPII cleft, and directly clashes with the H1 bound to the nucleosome. The transcription elongation factor Spt4/5 masks the RNAPII DNA binding region, and drastically reduces the H1-mediated RNAPII pausing.
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