Evidence map›Paper›PMID 25367076›Full record

ArticleMolecular microbiology2015

Determinants governing ligand specificity of the Vibrio harveyi LuxN quorum-sensing receptor.

Xiaobo Ke, Laura C Miller, Bonnie L Bassler

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Mechanism underlying autoinducer recognition in theThe Journal of biological chemistry · 2020
    Article
  10. Article
  11. Article
  12. Structural determinants driving homoserine lactone ligand selection in theProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Review
  15. Article
  16. Facultative cheating supports the coexistence of diverse quorum-sensing alleles.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Review
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

3 authors at 1 institution in 1 country.

Xiaobo KeDepartment of Molecular Biology, Princeton University, Princeton, NJ, 08540, USA.
Laura C Miller
Bonnie L Bassler
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Intra-and Inter-Species Communication in BacteriaR01GM065859 · NIGMS · PRINCETON UNIVERSITY · PI BASSLER, BONNIE L · 2002 to 2015
$4.2M
Howard Hughes Medical InstituteNIGMS NIH HHS 5R01GM065859NIGMS NIH HHS R01 GM065859NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Quorum sensing is a process of bacterial cell-cell communication that relies on the production, release and receptor-driven detection of extracellular signal molecules called autoinducers. The quorum-sensing bacterium Vibrio harveyi exclusively detects the autoinducer N-((R)-3-hydroxybutanoyl)-L-homoserine lactone (3OH-C4 HSL) via the two-component receptor LuxN. To discover the principles underlying the exquisite selectivity LuxN has for its ligand, we identified LuxN mutants with altered specificity. LuxN uses three mechanisms to verify that the bound molecule is the correct ligand: in the context of the overall ligand-binding site, His210 validates the C3 modification, Leu166 surveys the chain-length and a strong steady-state kinase bias imposes an energetic hurdle for inappropriate ligands to elicit signal transduction. Affinities for the LuxN kinase on and kinase off states underpin whether a ligand will act as an antagonist or an agonist. Mutations that bias LuxN to the agonized, kinase off, state are clustered in a region adjacent to the ligand-binding site, suggesting that this region acts as the switch that triggers signal transduction. Together, our analyses illuminate how a histidine sensor kinase differentiates between ligands and exploits those differences to regulate its signaling activity.

Indexed as

4-ButyrolactoneBacterial ProteinsBinding SitesHistidineLeucineProtein KinasesQuorum SensingSignal TransductionSubstrate SpecificityTranscription FactorsVibrio4-ButyrolactoneBacterial ProteinsHistidinehomoserine lactoneLeucineluxN protein, Vibrio harveyiProtein KinasesTranscription Factors

Identifiers

PMID25367076
PMCPMC4275348
OpenAlexW2126903952

What OpenQuestion holds

Textmetadata
LicenceTDM
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.