ArticleNucleic acids research2010
Rearrangement of the RNA polymerase subunit H and the lower jaw in archaeal elongation complexes.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Molecular Evolution of the Archaeal DNA-Dependent RNA Polymerase: Cooperative Changes in Subunit Composition and Specific Domains of Small Subunits.International journal of molecular sciences · 2026Article
- Displacement of the transcription factor B reader domain during transcription initiation.Nucleic acids research · 2018Article
- Rpb5, a subunit shared by eukaryotic RNA polymerases, cooperates with prefoldin-like Bud27/URI.AIMS genetics · 2018Review
- Transcription Regulation in Archaea.Journal of bacteriology · 2016Review
- Complete architecture of the archaeal RNA polymerase open complex from single-molecule FRET and NPS.Nature communications · 2015Article
- Article
- The RNA polymerase trigger loop functions in all three phases of the transcription cycle.Nucleic acids research · 2013Article
- Evolution of multisubunit RNA polymerases in the three domains of life.Nature reviews. Microbiology · 2011Review
- Fidelity in archaeal information processing.Archaea (Vancouver, B.C.) · 2010Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The lower jaws of archaeal RNA polymerase and eukaryotic RNA polymerase II include orthologous subunits H and Rpb5, respectively. The tertiary structure of H is very similar to the structure of the C-terminal domain of Rpb5, and both subunits are proximal to downstream DNA in pre-initiation complexes. Analyses of reconstituted euryarchaeal polymerase lacking subunit H revealed that H is important for open complex formation and initial transcription. Eukaryotic Rpb5 rescues activity of the DeltaH enzyme indicating a strong conservation of function for this subunit from archaea to eukaryotes. Photochemical cross-linking in elongation complexes revealed a striking structural rearrangement of RNA polymerase, bringing subunit H near the transcribed DNA strand one helical turn downstream of the active center, in contrast to the positioning observed in preinitiation complexes. The rearrangement of subunits H and A'' suggest a major conformational change in the archaeal RNAP lower jaw upon formation of the elongation complex.
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Registered trials
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