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The cutting edge of archaeal transcription

Fouqueau, T; Blombach, F; Cackett, G; Carty, AE; Matelska, DM; Ofer, S; Pilotto, S; ... Werner, F; + view all (2018) The cutting edge of archaeal transcription. Emerging Topics in Life Sciences , 2 (4) pp. 517-533. 10.1042/ETLS20180014. Green open access

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Abstract

The archaeal RNA polymerase (RNAP) is a double-psi β-barrel enzyme 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. Understanding archaeal transcription is, therefore, key to delineate the universally conserved fundamental mechanisms of transcription as well as the evolution of the archaeo-eukaryotic transcription machineries. The dynamic interplay between RNAP subunits, transcription factors and nucleic acids dictates the activity of RNAP and ultimately gene expression. This review focusses on recent progress in our understanding of (i) the structure, function and molecular mechanisms of known and less characterized factors including Elf1 (Elongation factor 1), NusA (N-utilization substance A), TFS4, RIP and Eta, and (ii) their evolution and phylogenetic distribution across the expanding tree of Archaea.ATV, Acidianus two-tailed virus; CC, closed; CRISPR, Clustered Regularly Interspaced Short Palindromic Repeats; DPBB, double-psi β-barrel; ECs, elongation complexes; Elf1, Elongation factor 1; Eta, Euryarchaeal Termination Activity; IMR, initially melted region; Inr, initiator; KOW, Kyrpides–Ouzounis–Woese; NTD, N-terminal domain; NTS, non-template strand; NusA, N-utilization substance A; OB, oligonucleotide/oligosaccharide binding; OC, open complex; PIC, pre-initiation complex; RIP, RNAP inhibitory protein; RNAP, RNA polymerase; STIV, Sulfolobusturreted icosahedral virus; TBP, TATA-binding protein; TFB, transcription factor B; TFE, transcription factor E; WH, winged helix

Type: Article
Title: The cutting edge of archaeal transcription
Open access status: An open access version is available from UCL Discovery
DOI: 10.1042/ETLS20180014
Publisher version: https://doi.org/10.1042/ETLS20180014
Language: English
Additional information: © 2018 The Author(s) This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and the Royal Society of Biology and distributed under the Creative Commons Attribution License 4.0 (CC BY) https://creativecommons.org/licenses/by/4.0/
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10066985
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