Structural basis of RNA polymerase inhibition by viral and host factors

Simona Pilotto, Thomas Fouqueau, Natalya Lukoyanova, Carol Sheppard, Soizick Lucas-Staat, Luis Miguel Díaz-Santín, Dorota Matelska, David Prangishvili, Alan C. M. Cheung and Finn Werner ()
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Simona Pilotto: University College London
Thomas Fouqueau: University College London
Natalya Lukoyanova: Birkbeck College
Carol Sheppard: Imperial College London
Soizick Lucas-Staat: Institut Pasteur
Luis Miguel Díaz-Santín: Birkbeck College
Dorota Matelska: University College London
David Prangishvili: Ivane Javakhishvili Tbilisi State University
Alan C. M. Cheung: University of Bristol
Finn Werner: University College London

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract RNA polymerase inhibition plays an important role in the regulation of transcription in response to environmental changes and in the virus-host relationship. Here we present the high-resolution structures of two such RNAP-inhibitor complexes that provide the structural bases underlying RNAP inhibition in archaea. The Acidianus two-tailed virus encodes the RIP factor that binds inside the DNA-binding channel of RNAP, inhibiting transcription by occlusion of binding sites for nucleic acid and the transcription initiation factor TFB. Infection with the Sulfolobus Turreted Icosahedral Virus induces the expression of the host factor TFS4, which binds in the RNAP funnel similarly to eukaryotic transcript cleavage factors. However, TFS4 allosterically induces a widening of the DNA-binding channel which disrupts trigger loop and bridge helix motifs. Importantly, the conformational changes induced by TFS4 are closely related to inactivated states of RNAP in other domains of life indicating a deep evolutionary conservation of allosteric RNAP inhibition.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25666-5

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DOI: 10.1038/s41467-021-25666-5

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