Evidence map›Paper›PMID 32662815›Full record

ArticleThe Biochemical journal2020

Activation by NarL at the Escherichia coli ogt promoter.

Patcharawarin Ruanto, David L Chismon, Joanne Hothersall, Rita E Godfrey, David J Lee, Stephen J W Busby, Douglas F Browning

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Transcription activation inEcoSal Plus · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
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

7 authors at 2 institutions in 1 country.

Patcharawarin RuantoInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
David L ChismonInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Joanne HothersallInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Rita E GodfreyInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
David J LeeInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Stephen J W BusbyInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Douglas F BrowningInstitute of Microbiology and Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
University of Birmingham · GBBirmingham City University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M018261/1Biotechnology and Biological Sciences Research Council BB/R017689/1Biotechnology and Biological Sciences Research Council BB/S506709/1
6 · The paper itself

Abstract

The Escherichia coli NarX/NarL two-component response-regulator system regulates gene expression in response to nitrate ions and the NarL protein is a global transcription factor, which activates transcript initiation at many target promoters. One such target, the E. coli ogt promoter, which controls the expression of an O6-alkylguanine-DNA-alkyltransferase, is dependent on NarL binding to two DNA targets centred at positions -44.5 and -77.5 upstream from the transcript start. Here, we describe ogt promoter derivatives that can be activated solely by NarL binding either at position -44.5 or position -77.5. We show that NarL can also activate the ogt promoter when located at position -67.5. We present data to argue that NarL-dependent activation of transcript initiation at the ogt promoter results from a direct interaction between NarL and a determinant in the C-terminal domain of the RNA polymerase α subunit. Footprinting experiments show that, at the -44.5 promoter, NarL and the C-terminal domain of the RNA polymerase α subunit bind to opposite faces of promoter DNA, suggesting an unusual mechanism of transcription activation. Our work suggests new organisations for activator-dependent transcription at promoters and future applications for biotechnology.

Indexed as

Promoter Regions, GeneticDNA-Binding ProteinsDNA-Directed RNA PolymerasesEscherichia coli K12Escherichia coli ProteinsGene Expression Regulation, BacterialMethyltransferasesNitratesTranscription Initiation, GeneticDNA-Binding ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsMethyltransferasesNarL protein, E coliNitratesOgt protein, E coliRNA polymerase alpha subunitmolecular interactionsNarLpromoterstranscription activation

Identifiers

PMID32662815
PMCPMC7419079
OpenAlexW3042878854

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.