Evidence map›Paper›PMID 25225400›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2.

João C Marques, Il Kyu Oh, Daniel C Ly, Pedro Lamosa, M Rita Ventura, Stephen T Miller, Karina B Xavier

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. 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
2.3field-weighted citation impact, top 11% 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, 58 citations in OpenAlex.

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  14. An Efficient Synthesis of Optically Active [4-Molecules (Basel, Switzerland) · 2021
    Article
  15. Article
  16. Article
  17. CRISPR-Pathogens (Basel, Switzerland) · 2020
    Article
  18. Article
  19. Article
  20. Identification of novel autoinducer-2 receptors inThe Journal of biological chemistry · 2019
    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 at 3 institutions in 2 countries.

João C MarquesInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal; Champalimaud Neuroscience Programme, Champalimaud Centre for the Unknown, Av. de Brasilia, 1400-038 Lisbon, Portugal;
Il Kyu OhDepartment of Chemistry and Biochemistry, Swarthmore College, Swarthmore, PA 19081; and.
Daniel C LyDepartment of Chemistry and Biochemistry, Swarthmore College, Swarthmore, PA 19081; and.
Pedro LamosaInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal.
M Rita VenturaInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal.
Stephen T MillerDepartment of Chemistry and Biochemistry, Swarthmore College, Swarthmore, PA 19081; and smiller1@swarthmore.edu kxavier@igc.gulbenkian.pt.
Karina B XavierInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal smiller1@swarthmore.edu kxavier@igc.gulbenkian.pt.ORCID http://orcid.org/0000-0001-5210-1434
Swarthmore College · USInstituto Gulbenkian de Ciência · PTUniversidade Nova de Lisboa · PT

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Structural and functional studies of autoinducer-2 processing proteinsR15GM096478 · NIGMS · SWARTHMORE COLLEGE · PI MILLER, STEPHEN T. · 2012 to 2012
$256k
Howard Hughes Medical Institute HHMI 55007436NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R15 GM096478NIGMS NIH HHS R15GM096478-01A1
6 · The paper itself

Abstract

The quorum sensing signal autoinducer-2 (AI-2) regulates important bacterial behaviors, including biofilm formation and the production of virulence factors. Some bacteria, such as Escherichia coli, can quench the AI-2 signal produced by a variety of species present in the environment, and thus can influence AI-2-dependent bacterial behaviors. This process involves uptake of AI-2 via the Lsr transporter, followed by phosphorylation and consequent intracellular sequestration. Here we determine the metabolic fate of intracellular AI-2 by characterizing LsrF, the terminal protein in the Lsr AI-2 processing pathway. We identify the substrates of LsrF as 3-hydroxy-2,4-pentadione-5-phosphate (P-HPD, an isomer of AI-2-phosphate) and coenzyme A, determine the crystal structure of an LsrF catalytic mutant bound to P-HPD, and identify the reaction products. We show that LsrF catalyzes the transfer of an acetyl group from P-HPD to coenzyme A yielding dihydroxyacetone phosphate and acetyl-CoA, two key central metabolites. We further propose that LsrF, despite strong structural homology to aldolases, acts as a thiolase, an activity previously undescribed for this family of enzymes. With this work, we have fully characterized the biological pathway for AI-2 processing in E. coli, a pathway that can be used to quench AI-2 and control quorum-sensing-regulated bacterial behaviors.

Indexed as

AcetyltransferasesAmino Acid SubstitutionCarrier ProteinsCoenzyme AEscherichia coliEscherichia coli ProteinsHomoserineKineticsLactonesModels, MolecularMutagenesis, Site-DirectedProtein ConformationProtein Processing, Post-TranslationalQuorum SensingAcetyltransferasesCarrier ProteinsCoenzyme AEscherichia coli ProteinsHomoserineLactonesLsrB protein, E coliN-octanoylhomoserine lactonebacterial communicationcell–cell signalingmetabolic fluxquorum quenching

Identifiers

PMID25225400
PMCPMC4191781
OpenAlexW2123087277

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.