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Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP

Author

Listed:
  • Carol Sheppard

    (Institute of Structural and Molecular Biology, University College London)

  • Fabian Blombach

    (Institute of Structural and Molecular Biology, University College London)

  • Adam Belsom

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Sarah Schulz

    (Physikalische und Theoretische Chemie—NanoBioSciences, Technische Universität Braunschweig)

  • Tina Daviter

    (Institute of Structural and Molecular Biology, University College London)

  • Katherine Smollett

    (Institute of Structural and Molecular Biology, University College London)

  • Emilie Mahieu

    (Institute of Structural and Molecular Biology, University College London)

  • Susanne Erdmann

    (University of Copenhagen)

  • Philip Tinnefeld

    (Physikalische und Theoretische Chemie—NanoBioSciences, Technische Universität Braunschweig)

  • Roger Garrett

    (University of Copenhagen)

  • Dina Grohmann

    (Physikalische und Theoretische Chemie—NanoBioSciences, Technische Universität Braunschweig
    Present address: Department of Microbiology and Archaea Centre, Laboratory of Single-Molecule Biochemistry, University of Regensburg, Regensburg 93053, Germany)

  • Juri Rappsilber

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh
    Institute of Biotechnology, Technische Universität Berlin)

  • Finn Werner

    (Institute of Structural and Molecular Biology, University College London)

Abstract

Little is known about how archaeal viruses perturb the transcription machinery of their hosts. Here we provide the first example of an archaeo-viral transcription factor that directly targets the host RNA polymerase (RNAP) and efficiently represses its activity. ORF145 from the temperate Acidianus two-tailed virus (ATV) forms a high-affinity complex with RNAP by binding inside the DNA-binding channel where it locks the flexible RNAP clamp in one position. This counteracts the formation of transcription pre-initiation complexes in vitro and represses abortive and productive transcription initiation, as well as elongation. Both host and viral promoters are subjected to ORF145 repression. Thus, ORF145 has the properties of a global transcription repressor and its overexpression is toxic for Sulfolobus. On the basis of its properties, we have re-named ORF145 RNAP Inhibitory Protein (RIP).

Suggested Citation

  • Carol Sheppard & Fabian Blombach & Adam Belsom & Sarah Schulz & Tina Daviter & Katherine Smollett & Emilie Mahieu & Susanne Erdmann & Philip Tinnefeld & Roger Garrett & Dina Grohmann & Juri Rappsilber, 2016. "Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP," Nature Communications, Nature, vol. 7(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13595
    DOI: 10.1038/ncomms13595
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