Evidence map›Paper›PMID 29679003›Full record

ArticleNature communications2018

The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage.

Han N Ho, Antoine M van Oijen, Harshad Ghodke

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  7. Oxidative stress drives mutagenesis through transcription-coupled repair in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  18. Mfd regulates RNA polymerase association with hard-to-transcribe regions in vivo, especially those with structured RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Han N HoSchool of Chemistry, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia.ORCID http://orcid.org/0000-0002-4583-1807
Antoine M van OijenSchool of Chemistry, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia.ORCID http://orcid.org/0000-0002-1794-5161
Harshad GhodkeSchool of Chemistry, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia. harshad@uow.edu.au.ORCID http://orcid.org/0000-0002-6628-876X
University of Wollongong · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During transcription elongation, bacterial RNA polymerase (RNAP) can pause, backtrack or stall when transcribing template DNA. Stalled transcription elongation complexes at sites of bulky lesions can be rescued by the transcription terminator Mfd. The molecular mechanisms of Mfd recruitment to transcription complexes in vivo remain to be elucidated, however. Using single-molecule live-cell imaging, we show that Mfd associates with elongation transcription complexes even in the absence of exogenous genotoxic stresses. This interaction requires an intact RNA polymerase-interacting domain of Mfd. In the presence of drugs that stall RNAP, we find that Mfd associates pervasively with RNAP. The residence time of Mfd foci reduces from 30 to 18 s in the presence of endogenous UvrA, suggesting that UvrA promotes the resolution of Mfd-RNAP complexes on DNA. Our results reveal that RNAP is frequently rescued by Mfd during normal growth and highlight a ubiquitous house-keeping role for Mfd in regulating transcription elongation.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsDNA, BacterialDNA-Binding ProteinsDNA-Directed RNA PolymerasesDNA RepairEscherichia coli K12Escherichia coli ProteinsTranscription FactorsTranscription, GeneticAdenosine TriphosphatasesBacterial ProteinsDNA, BacterialDNA-Binding ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsTranscription Factorstranscription repair coupling factor protein, BacteriaUvrA protein, E coli

Identifiers

PMID29679003
PMCPMC5910403
OpenAlexW2801044976

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.