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

2014Journal article Open access
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dc.contributor.authorMarques, João C.
dc.contributor.authorOh, Il Kyu
dc.contributor.authorLy, Daniel C.
dc.contributor.authorLamosa, Pedro
dc.contributor.authorVentura, M. Rita
dc.contributor.authorMiller, Stephen T.
dc.contributor.authorXavier, Karina Bivar
dc.date.accessioned2020-03-18T15:03:03Z
dc.date.available2020-03-18T15:03:03Z
dc.date.issued2014
dc.description.abstractThe 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.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1073/pnas.1408691111pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/943
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNational Academy of Sciencespt_PT
dc.relationFCTpt_PT
dc.relationStudies on the structure/activity relationship of AI-2, a bacterial signalling molecule for inter-species communication.
dc.relation.publisherversionhttps://www.pnas.org/content/111/39/14235pt_PT
dc.subjectAcetyltransferasespt_PT
dc.subjectAmino Acid Substitutionpt_PT
dc.subjectCarrier Proteinspt_PT
dc.subjectCoenzyme Apt_PT
dc.subjectEscherichia colipt_PT
dc.subjectEscherichia coli Proteinspt_PT
dc.subjectHomoserinept_PT
dc.subjectKineticspt_PT
dc.subjectLactonespt_PT
dc.subjectModels, Molecularpt_PT
dc.subjectMutagenesis, Site-Directedpt_PT
dc.subjectProtein Conformationpt_PT
dc.subjectProtein Processing, Post-Translationalpt_PT
dc.subjectQuorum Sensingpt_PT
dc.titleLsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2pt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleStudies on the structure/activity relationship of AI-2, a bacterial signalling molecule for inter-species communication.
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F113880%2F2009/PT
oaire.citation.endPage14240pt_PT
oaire.citation.issue39pt_PT
oaire.citation.startPage14235pt_PT
oaire.citation.titleProceedings of the National Academy of Sciencespt_PT
oaire.citation.volume111pt_PT
oaire.fundingStream3599-PPCDT
person.familyNameXavier
person.givenNameKarina
person.identifier.ciencia-id641F-7328-B863
person.identifier.orcid0000-0001-5210-1434
person.identifier.ridB-9425-2008
person.identifier.scopus-author-id6603926993
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication26248334-983e-47c9-b1af-769585eec81b
relation.isAuthorOfPublication.latestForDiscovery26248334-983e-47c9-b1af-769585eec81b
relation.isProjectOfPublicationbfad3798-25ea-4d71-84d9-86f2fc1bb2a6
relation.isProjectOfPublication.latestForDiscoverybfad3798-25ea-4d71-84d9-86f2fc1bb2a6

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