Evidence map›Paper›PMID 29186528›Full record

ArticleNucleic acids research2018

Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator.

Patricia Casino, Laura Miguel-Romero, Juanjo Huesa, Pablo García, Francisco García-Del Portillo, Alberto Marina

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
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  7. Impact ofEvolution letters · 2022
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  12. RcsAB and Fur Coregulate the Iron-Acquisition System viaFrontiers in cellular and infection microbiology · 2020
    Article
  13. Article
  14. Single-stranded telomere-binding protein employs a dual rheostat for binding affinity and specificity that drives function.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. 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

6 authors at 4 institutions in 1 country.

Patricia CasinoDepartamento de Bioquímica y Biología Molecular, Universitat de València, Dr Moliner 50, 46100 Burjassot, Spain.
Laura Miguel-RomeroDepartment of Genomic and Proteomic, Instituto de Biomedicina de Valencia (IBV-CSIC), Jaume Roig 11, 46010 Valencia, Spain.
Juanjo HuesaDepartamento de Bioquímica y Biología Molecular, Universitat de València, Dr Moliner 50, 46100 Burjassot, Spain.
Pablo GarcíaLaboratorio de Patógenos Bacterianos Intracelulares, Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología (CNB-CSIC), Darwin, 3. 28049 Madrid, Spain.
Francisco García-Del PortilloLaboratorio de Patógenos Bacterianos Intracelulares, Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología (CNB-CSIC), Darwin, 3. 28049 Madrid, Spain.
Alberto MarinaDepartment of Genomic and Proteomic, Instituto de Biomedicina de Valencia (IBV-CSIC), Jaume Roig 11, 46010 Valencia, Spain.
Centro Nacional de Biotecnología · ESUniversitat de València · ESInstituto de Biomedicina de Valencia · ESInstituto de Salud Carlos III · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RcsCDB phosphorelay system controls an extremely large regulon in Enterobacteriaceae that involves processes such as biofilm formation, flagella production, synthesis of extracellular capsules and cell division. Therefore, fine-tuning of this system is essential for virulence in pathogenic microorganisms of this group. The final master effector of the RcsCDB system is the response regulator (RR) RcsB, which activates or represses multiple genes by binding to different promoter regions. This regulatory activity of RcsB can be done alone or in combination with additional transcriptional factors in phosphorylated or dephosphorylated states. The capacity of RcsB to interact with multiple promoters and partners, either dephosphorylated or phosphorylated, suggests an extremely conformational dynamism for this RR. To shed light on the activation mechanism of RcsB and its implication on promoter recognition, we solved the crystal structure of full-length RcsB from Salmonella enterica serovar Typhimurium in the presence and absence of a phosphomimetic molecule BeF3-. These two novel structures have guided an extensive site-directed mutagenesis study at the structural and functional level that confirms RcsB conformational plasticity and dynamism. Our data allowed us to propose a β5-T switch mechanism where phosphorylation is coupled to alternative DNA binding ways and which highlights the conformational dynamism of RcsB to be so pleiotropic.

Indexed as

Nucleic Acid ConformationProtein DomainsAmino Acid SequenceBacterial ProteinsCrystallography, X-RayDNAModels, MolecularPhosphorylationProtein BindingSalmonella typhimuriumSequence Homology, Amino AcidBacterial ProteinsDNARcsB protein, Bacteria

Identifiers

PMID29186528
PMCPMC5758874
OpenAlexW2770736990

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.