Structure and function of archaeal RNA polymerases

@article{Werner2007StructureAF,
  title={Structure and function of archaeal RNA polymerases},
  author={Finn Werner},
  journal={Molecular Microbiology},
  year={2007},
  volume={65}
}
  • F. Werner
  • Published 1 September 2007
  • Biology
  • Molecular Microbiology
RNA polymerases (RNAPs) are essential to all life forms and therefore deserve our special attention. The archaeal RNAP is closely related to eukaryotic RNAPII in terms of subunit composition and architecture, promoter elements and basal transcription factors required for the initiation and elongation phase of transcription. RNAPs of this class are large and sophisticated enzymes that interact in a complex manner with DNA/RNA scaffolds, substrates NTPs and a plethora of transcription factors… 
View on Wiley
onlinelibrary.wiley.com
102 Citations
Highly Influential Citations
12
Background Citations
53
Methods Citations
1

102 Citations

Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure

TLDR
The structure of the 13-subunit DNA-directed RNAP from Sulfolobus shibatae is determined and subunit Rpo13, an RNAP component in the order Solfolobales, which contains a helix-turn-helix motif that interacts with the RpoH/Rpb5 and RpoA′/RPB1 subunits suggest a role in the formation of the transcription bubble.

Cycling through transcription with the RNA polymerase F/E (RPB4/7) complex: structure, function and evolution of archaeal RNA polymerase.

Molecular mechanisms of archaeal RNA polymerase.

TLDR
The recent development of methods to reconstitute archaeal RNAP from recombinant materials in conjunction with structural information of multisubunit RNAPs present a potent opportunity to investigate the molecular mechanisms of transcription.

RNA-binding to archaeal RNA polymerase subunits F/E: a DEER and FRET study.

TLDR
Results demonstrate that, upon binding of RNA, F/E remains in a stable conformation, which suggests that it serves as a structurally rigid guiding rail for the growing RNA chain during transcription.

Evolutionary Origins of Two-Barrel RNA Polymerases and Site-Specific Transcription Initiation.

TLDR
This review focuses on recent insights into the evolution of the transcription apparatus with regard to the surprisingly pervasive double-Ψ β-barrel active-site configuration among different nucleic acid polymerase families.

Archaeal RNA polymerase and transcription regulation

TLDR
High-resolution X-ray crystal structures of archaeal RNAP allow a structural comparison of the transcription machinery among all three domains of life and suggest an intriguing hybrid of eukaryotic-type transcription apparatus and bacterial-like regulatory mechanisms in archaea.

Evolution of multisubunit RNA polymerases in the three domains of life

TLDR
An overview of the evolutionary conservation of and differences between the multisubunit polymerases in the three domains of life is provided, and the 'elongation first' hypothesis for the evolution of transcriptional regulation is introduced.

RNAP subunits F/E (RPB4/7) are stably associated with archaeal RNA polymerase: using fluorescence anisotropy to monitor RNAP assembly in vitro.

TLDR
The molecular interactions between the F/E complex and the RNAP core are characterized and it is shown that F/e binds to RNAP with submicromolar affinity and is not in a dynamic exchange with unbound F/ E.

Biogenesis of RNA Polymerases in Yeast

TLDR
This study reviews the latest studies governing the mechanisms and proteins described as being involved in the biogenesis of RNA polymerases in yeast by characterizing some elements involved inThe assembly of these multisubunit complexes.

Biogenesis of multisubunit RNA polymerases.

...

References

SHOWING 1-10 OF 74 REFERENCES

A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription.

Structure of an archaeal homolog of the eukaryotic RNA polymerase II RPB4/RPB7 complex.

Rpb4 and Rpb7: subunits of RNA polymerase II and beyond.

  • M. Choder
  • Biology
    Trends in biochemical sciences
  • 2004

Transcription Factor S, a Cleavage Induction Factor of the Archaeal RNA Polymerase*

TLDR
In vitro transcription experiments with paused elongation complexes at position +25 showed that TFS is able to induce cleavage activity in the archaeal RNA polymerase in a similar manner to TFIIS.

A Fully Recombinant System for Activator-dependent Archaeal Transcription*

TLDR
The construction of an entirely recombinant system for positively regulated archaeal transcription by omitting individual subunits from the in vitro assembly of the 12-subunit RNA polymerase from the hyperthermophile Methanocaldococcus jannaschii is reported.

Direct Modulation of RNA Polymerase Core Functions by Basal Transcription Factors

TLDR
TFB mutations are complemented by TFE, thereby demonstrating that both factors act synergistically during transcription initiation, and an additional function of TFE is to dynamically alter the nucleic acid-binding properties of RNAP by stabilizing the initiation complex and destabilizing elongation complexes.

Structural basis for transcription elongation by bacterial RNA polymerase

TLDR
The 2.5-Å resolution structure of the Thermus thermophilus EC is reported; the structure reveals the post-translocated intermediate with the DNA template in the active site available for pairing with the substrate.

The orientation of DNA in an archaeal transcription initiation complex

TLDR
A photochemical crosslinking method was used to map the vicinity of the catalytic subunits of Pfu RNA polymerase to DNA locations distributed along the polymerase–promoter interface and specifies the directionality of DNA in the archaeal transcription complex and its trajectory downstream of the transcriptional start site.

The RNA polymerase II elongation complex

TLDR
Recent insights into the structures and functions of RNA polymerase II and the transcription factors that control its activity during the elongation stage of eukaryotic messenger RNA synthesis are described.

RNA polymerase II structure: from core to functional complexes.

  • P. Cramer
  • Biology
    Current opinion in genetics & development
  • 2004
...