The X-ray crystal structure of RNA polymerase from Archaea

@article{Hirata2008TheXC,
  title={The X-ray crystal structure of RNA polymerase from Archaea},
  author={Akira Hirata and Brianna J. Klein and Katsuhiko S. Murakami},
  journal={Nature},
  year={2008},
  volume={451},
  pages={851-854}
}
The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of… 
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Recombinant archaeal RNAPs lacking specific subunits were used to investigate the functions of smaller subunits and revealed that the subunits P and H, the orthologues of eukaryotic Rpb12 and Rpb5, were not required for RNAP assembly, and subunit P was essential for open complex formation.
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TLDR
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TLDR
Compared with models of the eukaryotic OC, the TATA DNA region with TBP and TFB is positioned closer to the surface of the RNAP, likely providing the mechanism by which DNA melting can occur in a minimal factor configuration, without the dedicated translocase/helicase encoding factor TFIIH.
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TLDR
To understand the structure and function of archaeal RNAP, the TON-0309 gene encoding DNA-directed RNA polymerase subunit L (ToRNAP_L) from Thermococcus onnurineus NA1 was cloned and the protein was overexpressed in Escherichia coli, purified and crystallized.
Structure and Function of RNA Polymerases and the Transcription Machineries.
TLDR
The three-dimensional organisation of RNAPs from the bacterial, archaeal and eukaryotic domains of life is discussed, highlighting the conserved nature, but also the domain-specific features of the transcriptional apparatus.
Archaeal transcription: making up for lost time.
TLDR
A novel atomic model of SshRNAP (Sulfolobus shibatae RNAP) in complex with dsDNA (double-stranded DNA) constitutes a new piece of information helping the understanding of the mechanisms for DNA stabilization at the position downstream of the catalytic site during transcription.
Crystal structure of the 14-subunit RNA polymerase I
TLDR
The crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk, and an extended loop mimics the DNA backbone in the clefts and may be involved in regulating Pol I transcription.
Nanomechanical constraints acting on the catalytic site of cellular RNA polymerases.
  • R. Weinzierl
  • Biology, Chemistry
    Biochemical Society transactions
  • 2010
TLDR
It is demonstrated that the bridge-helix undergoes substantial conformational changes within a narrowly confined region (mjA' Ala(822)-Gln(823)-Ser(824)) during the nucleotide-addition cycle, suggesting that the RNAP active site is conformationally constrained.
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