Evidence map›Paper›PMID 29487239›Full record

ArticlemBio2018

Structural Basis for DNA Recognition by the Two-Component Response Regulator RcsB.

Ekaterina V Filippova, Bozena Zemaitaitis, Theint Aung, Alan J Wolfe, Wayne F Anderson

Abstract read
In one paragraph

Article in mBio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Antiviral Activity ofAntimicrobial agents and chemotherapy · 2023
    Article
  6. TheJournal of bacteriology · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. RcsAB and Fur Coregulate the Iron-Acquisition System viaFrontiers in cellular and infection microbiology · 2020
    Article
  12. 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

5 authors.

Ekaterina V FilippovaCenter for Structural Genomics of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA e-filippova@northwestern.edu wf-anderson@northwestern.edu.
Bozena ZemaitaitisDepartment of Microbiology and Immunology, Loyola University Chicago, Health Sciences Division, Stritch School of Medicine, Maywood, Illinois, USA.
Theint AungKeck Biophysics Facility, Northwestern University, Evanston, Illinois, USA.
Alan J WolfeDepartment of Microbiology and Immunology, Loyola University Chicago, Health Sciences Division, Stritch School of Medicine, Maywood, Illinois, USA.
Wayne F AndersonCenter for Structural Genomics of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA e-filippova@northwestern.edu wf-anderson@northwestern.edu.

Funding

Regulatory Network of the Lyme Disease PathogenR01AI083640 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI X. Frank Yang · 2009 to 2026
$5.9M
NIAID NIH HHS HHSN272201700060CNIAID NIH HHS R01 AI083640
6 · The paper itself

Abstract

RcsB is a highly conserved transcription regulator of the Rcs phosphorelay system, a complex two-component signal transduction system (N. Majdalani and S. Gottesman, Annu Rev Microbiol 59:379-405, 2005; A. J. Wolfe, Curr Opin Microbiol 13:204-209, 2010, https://doi.org/10.1016/j.mib.2010.01.002; D. J. Clarke, Future Microbiol 5:1173-1184, 2010, https://doi.org/10.2217/fmb.10.83). RcsB plays an important role in virulence and pathogenicity in human hosts by regulating biofilm formation. RcsB can regulate transcription alone or together with its auxiliary transcription regulators by forming heterodimers. This complexity allows RcsB to regulate transcription of more than 600 bacterial genes in response to different stresses (D. Wang et al., Mol Plant Microbe Interact 25:6-17, 2012, https://doi.org/10.1094/MPMI-08-11-0207). Despite increasing knowledge of RcsB importance, molecular mechanisms that drive the ability of RcsB to control transcription of a large number of genes remain unclear. Here, we present crystal structures of unphosphorylated RcsB in complex with the consensus DNA-binding sequence of 22-mer (DNA22) and 18-mer (DNA18) of the

Indexed as

Crystallography, X-RayDNA, BacterialEscherichia coli ProteinsModels, MolecularProtein BindingProtein ConformationProtein MultimerizationTranscription FactorsDNA, BacterialEscherichia coli ProteinsRcsB protein, E coliTranscription FactorsDNA-binding proteinstranscriptiontwo-component signal transductionX-ray crystallography

Identifiers

PMID29487239
PMCPMC5829831

What OpenQuestion holds

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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.