Structure and function of archaeal RNA polymerases

@article{Werner2007StructureAF,
  title={Structure and function of archaeal RNA polymerases},
  author={F. Werner},
  journal={Molecular Microbiology},
  year={2007},
  volume={65}
}
  • F. Werner
  • Published 2007
  • Biology, Medicine
  • 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… Expand
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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. Expand
Cycling through transcription with the RNA polymerase F/E (RPB4/7) complex: structure, function and evolution of archaeal RNA polymerase.
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This review focuses on the multiple functions of the most prominent feature that differentiates these enzymes from the bacterial RNAP--a stalk-like protrusion, which consists of the heterodimeric F/E subcomplex. Expand
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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. Expand
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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. Expand
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. Expand
Archaeal RNA polymerase and transcription regulation
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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. Expand
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. Expand
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. Expand
Molecular mechanisms of RNA polymerase—the F/E (RPB4/7) complex is required for high processivity in vitro
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It is suggested that interactions between RNAP subunits F/E and the RNA transcript are pivotal to the molecular mechanisms of RNAP during transcription elongation and termination. Expand
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. Expand
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