ArticleNature communications2020
Direct binding of TFEα opens DNA binding cleft of RNA polymerase.
Article in Nature communications, 2020. 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.
- Promoter contacts by TFB and TFEα during archaeal transcription initiation.Transcription · 2026Article
- Single-stranded DNA drives σ subunit loading onto mycobacterial RNA polymerase to unlock initiation-competent conformations.Nucleic acids research · 2025Article
- Structural basis of RNA polymerase complexes in African swine fever virus.Nature communications · 2025Article
- Structural insights into distinct mechanisms of RNA polymerase II and III recruitment to snRNA promoters.Nature communications · 2025Article
- Article
- Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.Nucleic acids research · 2024Article
- The ancient Z-DNA and Z-RNA specific Zα fold has evolved modern roles in immunity and transcription through the natural selection of flipons.Royal Society open science · 2024Article
- Structure of the recombinant RNA polymerase from African Swine Fever Virus.Nature communications · 2024Article
- The structure and activities of the archaeal transcription termination factor Eta detail vulnerabilities of the transcription elongation complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of RNA polymerase inhibition by viral and host factors.Nature communications · 2021Article
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Authors and funding
7 authors.
Funding
Abstract
Opening of the DNA binding cleft of cellular RNA polymerase (RNAP) is necessary for transcription initiation but the underlying molecular mechanism is not known. Here, we report on the cryo-electron microscopy structures of the RNAP, RNAP-TFEα binary, and RNAP-TFEα-promoter DNA ternary complexes from archaea, Thermococcus kodakarensis (Tko). The structures reveal that TFEα bridges the RNAP clamp and stalk domains to open the DNA binding cleft. Positioning of promoter DNA into the cleft closes it while maintaining the TFEα interactions with the RNAP mobile modules. The structures and photo-crosslinking results also suggest that the conserved aromatic residue in the extended winged-helix domain of TFEα interacts with promoter DNA to stabilize the transcription bubble. This study provides a structural basis for the functions of TFEα and elucidates the mechanism by which the DNA binding cleft is opened during transcription initiation in the stalk-containing RNAPs, including archaeal and eukaryotic RNAPs.
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