Evidence map›Paper›PMID 28432336›Full record

ArticleScientific reports2017

Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator.

Andreas Schlundt, Sophie Buchner, Robert Janowski, Thomas Heydenreich, Ralf Heermann, Jürgen Lassak, Arie Geerlof, Ralf Stehle, Dierk Niessing, Kirsten Jung and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. A short history of Auto-Rickshaw.Acta crystallographica. Section D, Structural biology · 2026
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  8. Structural Insights into Regulation of Vibrio Virulence Gene Networks.Advances in experimental medicine and biology · 2023
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  15. 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

11 authors at 2 institutions in 1 country.

Andreas SchlundtMunich Center for Integrated Protein Science (CiPSM) at the Department of Chemistry, Technische Universität München, 85748, Garching, Germany.ORCID http://orcid.org/0000-0003-2254-7560
Sophie BuchnerMunich Center for Integrated Protein Science (CiPSM) at the Department of Microbiology, Ludwig-Maximilians-Universität München, 82152, Martinsried, Germany.
Robert JanowskiGroup Intracellular Transport and RNA Biology at the Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Thomas HeydenreichMunich Center for Integrated Protein Science (CiPSM) at the Department of Chemistry, Technische Universität München, 85748, Garching, Germany.ORCID http://orcid.org/0000-0003-0933-0703
Ralf HeermannMunich Center for Integrated Protein Science (CiPSM) at the Department of Microbiology, Ludwig-Maximilians-Universität München, 82152, Martinsried, Germany.
Jürgen LassakMunich Center for Integrated Protein Science (CiPSM) at the Department of Microbiology, Ludwig-Maximilians-Universität München, 82152, Martinsried, Germany.
Arie GeerlofInstitute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Ralf StehleMunich Center for Integrated Protein Science (CiPSM) at the Department of Chemistry, Technische Universität München, 85748, Garching, Germany.
Dierk NiessingGroup Intracellular Transport and RNA Biology at the Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.ORCID http://orcid.org/0000-0002-5589-369X
Kirsten JungMunich Center for Integrated Protein Science (CiPSM) at the Department of Microbiology, Ludwig-Maximilians-Universität München, 82152, Martinsried, Germany. Kirsten.Jung@lrz.uni-muenchen.de.
Michael SattlerMunich Center for Integrated Protein Science (CiPSM) at the Department of Chemistry, Technische Universität München, 85748, Garching, Germany. sattler@helmholtz-muenchen.de.ORCID http://orcid.org/0000-0002-1594-0527
Center for Integrated Protein Science Munich · DEHelmholtz Zentrum München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmembrane DNA-binding protein CadC of E. coli, a representative of the ToxR-like receptor family, combines input and effector domains for signal sensing and transcriptional activation, respectively, in a single protein, thus representing one of the simplest signalling systems. At acidic pH in a lysine-rich environment, CadC activates the transcription of the cadBA operon through recruitment of the RNA polymerase (RNAP) to the two cadBA promoter sites, Cad1 and Cad2, which are directly bound by CadC. However, the molecular details for its interaction with DNA have remained elusive. Here, we present the crystal structure of the CadC DNA-binding domain (DBD) and show that it adopts a winged helix-turn-helix fold. The interaction with the cadBA promoter site Cad1 is studied by using nuclear magnetic resonance (NMR) spectroscopy, biophysical methods and functional assays and reveals a preference for AT-rich regions. By mutational analysis we identify amino acids within the CadC DBD that are crucial for DNA-binding and functional activity. Experimentally derived structural models of the CadC-DNA complex indicate that the CadC DBD employs mainly non-sequence-specific over a few specific contacts. Our data provide molecular insights into the CadC-DNA interaction and suggest how CadC dimerization may provide high-affinity binding to the Cad1 promoter.

Indexed as

Gene Expression Regulation, BacterialAdenosine TriphosphatasesAmino Acid Transport SystemsAntiportersCrystallography, X-RayDNA, BacterialDNA Mutational AnalysisEscherichia coliEscherichia coli ProteinsHelix-Turn-Helix MotifsHydrogen-Ion ConcentrationMagnetic Resonance SpectroscopyModels, MolecularPromoter Regions, GeneticProtein BindingProtein ConformationAdenosine TriphosphatasesAmino Acid Transport SystemsAntiportersCadB protein, E ColiCadC protein, E colicadmium translocating ATPaseDNA, BacterialEscherichia coli ProteinsTrans-Activators

Identifiers

PMID28432336
PMCPMC5430869
OpenAlexW2606042832

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.