Evidence map›Paper›PMID 24617591›Full record

ArticleMolecular microbiology2014

The PAS domain-containing histidine kinase RpfS is a second sensor for the diffusible signal factor of Xanthomonas campestris.

Shi-Qi An, John H Allan, Yvonne McCarthy, Melanie Febrer, J Maxwell Dow, Robert P Ryan

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
9.3field-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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  5. A guide toFrontiers in cellular and infection microbiology · 2023
    Review
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  13. Review
  14. The roles of histidine kinases in sensing host plant and cell-cell communication signal in a phytopathogenic bacterium.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
  15. Article
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  18. 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

6 authors at 2 institutions in 2 countries.

Shi-Qi AnDivision of Molecular Microbiology, Colleges of Life Sciences, University of Dundee, Dundee, UK.
John H Allan
Yvonne McCarthy
Melanie Febrer
J Maxwell Dow
Robert P Ryan
University of Dundee · GBUniversity College Cork · IE

Funding

Wellcome Trust 100204Wellcome Trust WT093314MAWellcome Trust WT100204AIA
6 · The paper itself

Abstract

A cell-cell signalling system mediated by the fatty acid signal DSF controls the virulence of Xanthomonas campestris pv. campestris (Xcc) to plants. The synthesis and recognition of the DSF signal depends upon different Rpf proteins. DSF signal generation requires RpfF whereas signal perception and transduction depends upon the sensor RpfC and regulator RpfG. Detailed analyses of the regulatory roles of different Rpf proteins have suggested the occurrence of further sensors for DSF. Here we have used a mutagenesis approach coupled with high-resolution transcriptional analysis to identify XC_2579 (RpfS) as a second sensor for DSF in Xcc. RpfS is a complex sensor kinase predicted to have multiple Per/Arnt/Sim (PAS) domains, a histidine kinase domain and a C-terminal receiver (REC) domain. Isothermal calorimetry showed that DSF bound to the isolated N-terminal PAS domain with a Kd of 1.4 μM. RpfS controlled expression of a sub-set of genes distinct from those controlled by RpfC to include genes involved in type IV secretion and chemotaxis. Mutation of XC_2579 was associated with a reduction in virulence of Xcc to Chinese Radish when assayed by leaf spraying but not by leaf inoculation, suggesting a role for RpfS-controlled factors in the epiphytic phase of the disease cycle.

Indexed as

Gene Expression Regulation, BacterialFatty AcidsGene DeletionGene Expression ProfilingHistidine KinaseKineticsMutagenesis, InsertionalPlant DiseasesProtein BindingProtein KinasesRaphanusVirulenceXanthomonas campestrisFatty AcidsHistidine KinaseProtein Kinases

Identifiers

PMID24617591
PMCPMC4159695
OpenAlexW2121899890

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.