Evidence map›Paper›PMID 22155778›Full record

ArticleJournal of bacteriology2012

Mutation of the sensor kinase chvG in Rhizobium leguminosarum negatively impacts cellular metabolism, outer membrane stability, and symbiosis.

Elizabeth M Vanderlinde, Christopher K Yost

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

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  8. Global control of bacterial nitrogen and carbon metabolism by a PTSProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  11. Transcriptomic Studies Reveal that theInternational journal of molecular sciences · 2019
    Article
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  14. Article
  15. Mutation in theGenes · 2018
    Article
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  18. Review
  19. Article
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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

2 authors at 1 institution in 1 country.

Elizabeth M VanderlindeDepartment of Biology, University of Regina, Regina, Saskatchewan, Canada.
Christopher K Yost
University of Regina · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two-component signal transduction systems (TCS) are a main strategy used by bacteria to sense and adapt to changes in their environment. In the legume symbiont Rhizobium leguminosarum biovar viciae VF39, mutation of chvG, a histidine kinase, caused a number of pleiotropic phenotypes. ChvG mutants are unable to grow on proline, glutamate, histidine, or arginine as the sole carbon source. The chvG mutant secreted smaller amounts of acidic and neutral surface polysaccharides and accumulated abnormally large amounts of poly-ß-hydroxybutyrate. Mutation of chvG caused symbiotic defects on peas, lentils, and vetch; nodules formed by the chvG mutant were small and white and contained only a few cells that had failed to differentiate into bacteroids. Mutation of chvG also destabilized the outer membrane of R. leguminosarum, resulting in increased sensitivity to membrane stressors. Constitutive expression of ropB, the outer membrane protein-encoding gene, restored membrane stability and rescued the sensitivity phenotypes described above. Similar phenotypes have been described for mutations in other ChvG-regulated genes encoding a conserved operon of unknown function and in the fabXL genes required for synthesis of the lipid A very-long-chain fatty acid, suggesting that ChvG is a key component of the envelope stress response in Rhizobium leguminosarum. Collectively, the results of this study demonstrate the important and unique role the ChvG/ChvI TCS plays in the physiology, metabolism, and symbiotic competency of R. leguminosarum.

Indexed as

SymbiosisArginineBacterial Outer Membrane ProteinsBacterial ProteinsCell MembraneDNA, BacterialGenes, BacterialGlutamic AcidHistidineHydroxybutyratesLens PlantMutationPisum sativumPolyestersPolyhydroxybutyratesPolysaccharidesArginineBacterial Outer Membrane ProteinsBacterial ProteinschvG protein, BacteriachvI protein, BacteriaDNA, BacterialGlutamic AcidHistidineHydroxybutyratespoly-beta-hydroxybutyratePolyestersPolyhydroxybutyratesPolysaccharidesProlineProtein KinasesRopB protein, Rhizobium leguminosarumTranscription Factors

Identifiers

PMID22155778
PMCPMC3272964
OpenAlexW2122420189

What OpenQuestion holds

Textmetadata
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.