Abstract
In recent years, emerging structural information on the aRNAP (archaeal RNA polymerase) apparatus has shown its strong evolutionary relationship with the eukaryotic counterpart, RNA Pol (polymerase) II. 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. In Archaea, in contrast with Eukarya, downstream DNA stabilization is universally mediated by the jaw domain and, in some species, by the additional presence of the Rpo13 subunit. Biochemical and biophysical data, combined with X-ray structures of apo- and DNA-bound aRNAP, have demonstrated the capability of the Rpo13 C-terminus to bind in a sequence-independent manner to downstream DNA. In the present review, we discuss the recent findings on the aRNAP and focus on the mechanisms by which the RNAP stabilizes the bound DNA during transcription.
- Archaea
- RNA polymerase
- Rpo13
- transcription
- X-ray structure
Footnotes
Molecular Biology of Archaea 3: An Independent Meeting held at the Max Planck Institute for Terrestrial Microbiology, Marburg, Germany, 2–4 July 2012. Organized and Edited by Sonja-Verena Albers (Max Planck Institute for Terrestrial Microbiology, Germany), Bettina Siebers (University of Duisberg-Essen, Germany) and Finn Werner (University College London, U.K.).
Abbreviations: aRNAP, archaeal RNA polymerase; dsDNA, double-stranded DNA; electron, microscopy; eRNAP, eukaryotic RNA polymerase; LACA, last archaeal common ancestor; OC, open complex; PfuRNAP, Pyrococcus furiosus RNA polymerase; Pol, polymerase; RNAP, RNA polymerase; SshRNAP, Sulfolobus shibatae RNAP; TBP, TATA-box-binding protein; TEC, transcription elongation complex; TF, transcription factor
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