Evidence map›Paper›PMID 23677992›Full record

ArticleThe Journal of biological chemistry2013

High specificity in CheR methyltransferase function: CheR2 of Pseudomonas putida is essential for chemotaxis, whereas CheR1 is involved in biofilm formation.

Cristina García-Fontana, José Antonio Reyes-Darias, Francisco Muñoz-Martínez, Carlos Alfonso, Bertrand Morel, Juan Luis Ramos, Tino Krell

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Tylosin Removal Under PbAntioxidants (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Microbiology and molecular biology reviews : MMBR · 2021
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Sensory Repertoire of Bacterial Chemoreceptors.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  14. Assigning chemoreceptors to chemosensory pathways inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors.

Cristina García-FontanaDepartment of Environmental Protection, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, C/ Prof. Albareda, 1, 18008 Granada, Spain.
José Antonio Reyes-Darias
Francisco Muñoz-Martínez
Carlos Alfonso
Bertrand Morel
Juan Luis Ramos
Tino Krell

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chemosensory pathways are a major signal transduction mechanism in bacteria. CheR methyltransferases catalyze the methylation of the cytosolic signaling domain of chemoreceptors and are among the core proteins of chemosensory cascades. These enzymes have primarily been studied Escherichia coli and Salmonella typhimurium, which possess a single CheR involved in chemotaxis. Many other bacteria possess multiple cheR genes. Because the sequences of chemoreceptor signaling domains are highly conserved, it remains to be established with what degree of specificity CheR paralogues exert their activity. We report here a comparative analysis of the three CheR paralogues of Pseudomonas putida. Isothermal titration calorimetry studies show that these paralogues bind the product of the methylation reaction, S-adenosylhomocysteine, with much higher affinity (KD of 0.14-2.2 μM) than the substrate S-adenosylmethionine (KD of 22-43 μM), which indicates product feedback inhibition. Product binding was particularly tight for CheR2. Analytical ultracentrifugation experiments demonstrate that CheR2 is monomeric in the absence and presence of S-adenosylmethionine or S-adenosylhomocysteine. Methylation assays show that CheR2, but not the other paralogues, methylates the McpS and McpT chemotaxis receptors. The mutant in CheR2 was deficient in chemotaxis, whereas mutation of CheR1 and CheR3 had either no or little effect on chemotaxis. In contrast, biofilm formation of the CheR1 mutant was largely impaired but not affected in the other mutants. We conclude that CheR2 forms part of a chemotaxis pathway, and CheR1 forms part of a chemosensory route that controls biofilm formation. Data suggest that CheR methyltransferases act with high specificity on their cognate chemoreceptors.

Indexed as

BiofilmsAmino Acid SequenceBacterial ProteinsCalorimetryChemotaxisMethyltransferasesMolecular Sequence DataMutationOligonucleotidesProtein BindingProtein Interaction Domains and MotifsPseudomonas putidaS-AdenosylmethionineSequence Homology, Amino AcidSignal TransductionSubstrate SpecificityBacterial ProteinsCheR protein, Pseudomonas putidaMethyltransferasesOligonucleotidesS-AdenosylmethionineCalorimetryChemoreceptorChemotaxisCheR MethyltransferaseProtein MethylationPseudomonasReceptor ModificationReceptorsS-Adenosylmethionine (SAM)Signal Transduction

Identifiers

PMID23677992
PMCPMC3696673

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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.