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Ribosome reactivates transcription by physically pushing RNA polymerase out of transcription arrest

Lookup NU author(s): Dr Flint Stevenson-Jones, Dr Jason WoodgateORCiD, Daniel Castro-Roa, Professor Nikolay ZenkinORCiD



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


© This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY).In bacteria, the first two steps of gene expression-transcription and translation-are spatially and temporally coupled. Uncoupling may lead to the arrest of transcription through RNA polymerase backtracking, which interferes with replication forks, leading to DNA double-stranded breaks and genomic instability. How transcription-translation coupling mitigates these conflicts is unknown. Here we show that, unlike replication, translation is not inhibited by arrested transcription elongation complexes. Instead, the translating ribosome actively pushes RNA polymerase out of the backtracked state, thereby reactivating transcription. We show that the distance between the two machineries upon their contact on mRNA is smaller than previously thought, suggesting intimate interactions between them. However, this does not lead to the formation of a stable functional complex between the enzymes, as was once proposed. Our results reveal an active, energy-driven mechanism that reactivates backtracked elongation complexes and thus helps suppress their interference with replication.

Publication metadata

Author(s): Stevenson-Jones F, Woodgate J, Castro-Roa D, Zenkin N

Publication type: Article

Publication status: Published

Journal: Proceedings of the National Academy of Sciences of the United States of America

Year: 2020

Volume: 117

Issue: 15

Pages: 8462-8467

Print publication date: 14/04/2020

Online publication date: 01/01/2020

Acceptance date: 02/04/2016

Date deposited: 28/04/2020

ISSN (print): 0027-8424

ISSN (electronic): 1091-6490

Publisher: National Academy of Sciences


DOI: 10.1073/pnas.1919985117

PubMed id: 32238560


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Funder referenceFunder name
Leverhulme Trust Prize PLP-2014-229,
UK Biotechnology and Biological Sciences Research CouncilGrants BB/J006378/1
UK Engineering and Physical Sciences Research Council Grant EP/T002778/1
Wellcome Trust Investigator Awards 102851/Z/13/Z
UK Biotechnology and Biological Sciences Research CouncilGrants and 1237752 (to N.Z.)
Wellcome Trust Investigator Awards 217189/Z/19/Z