ArticleProceedings of the National Academy of Sciences of the United States of America2016
TFE and Spt4/5 open and close the RNA polymerase clamp during the transcription cycle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Promoter contacts by TFB and TFEα during archaeal transcription initiation.Transcription · 2026Article
- Structural insights into σ28-dependent transcription initiation and its regulation by anti-sigma factor in Pseudomonas aeruginosa.Nucleic acids research · 2026Article
- Single-stranded DNA drives σ subunit loading onto mycobacterial RNA polymerase to unlock initiation-competent conformations.Nucleic acids research · 2025Article
- Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.Nature structural & molecular biology · 2024Article
- Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.Nucleic acids research · 2024Article
- Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.bioRxiv : the preprint server for biology · 2024Article
- Mechanisms and Functions of the RNA Polymerase II General Transcription Machinery during the Transcription Cycle.Biomolecules · 2024Review
- Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization.Nature communications · 2023Article
- RNA Polymerase II "Pause" Prepares Promoters for Upcoming Transcription duringInternational journal of molecular sciences · 2022Article
- How to Shut Down Transcription in Archaea during Virus Infection.Microorganisms · 2022Review
- Single-molecule FRET uncovers hidden conformations and dynamics of human Argonaute 2.Nature communications · 2022Article
- Recruitment of Xrn1 to stress-induced genes allows efficient transcription by controlling RNA polymerase II backtracking.RNA biology · 2021Article
- Promoter-proximal elongation regulates transcription in archaea.Nature communications · 2021Article
- Structural basis of RNA polymerase inhibition by viral and host factors.Nature communications · 2021Article
- CDK9 keeps RNA polymerase II on track.Cellular and molecular life sciences : CMLS · 2021Review
- Opposite roles of transcription elongation factors Spt4/5 and Elf1 in RNA polymerase II transcription through B-form versus non-B DNA structures.Nucleic acids research · 2021Article
- Structure of the p53/RNA polymerase II assembly.Communications biology · 2021Article
- Direct binding of TFEα opens DNA binding cleft of RNA polymerase.Nature communications · 2020Article
- Archaeal transcription.Transcription · 2020Review
- Nucleotide Loading Modes of Human RNA Polymerase II as Deciphered by Molecular Simulations.Biomolecules · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
Abstract
Transcription is an intrinsically dynamic process and requires the coordinated interplay of RNA polymerases (RNAPs) with nucleic acids and transcription factors. Classical structural biology techniques have revealed detailed snapshots of a subset of conformational states of the RNAP as they exist in crystals. A detailed view of the conformational space sampled by the RNAP and the molecular mechanisms of the basal transcription factors E (TFE) and Spt4/5 through conformational constraints has remained elusive. We monitored the conformational changes of the flexible clamp of the RNAP by combining a fluorescently labeled recombinant 12-subunit RNAP system with single-molecule FRET measurements. We measured and compared the distances across the DNA binding channel of the archaeal RNAP. Our results show that the transition of the closed to the open initiation complex, which occurs concomitant with DNA melting, is coordinated with an opening of the RNAP clamp that is stimulated by TFE. We show that the clamp in elongation complexes is modulated by the nontemplate strand and by the processivity factor Spt4/5, both of which stimulate transcription processivity. Taken together, our results reveal an intricate network of interactions within transcription complexes between RNAP, transcription factors, and nucleic acids that allosterically modulate the RNAP during the transcription cycle.
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