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Chlamydomonas reinhardtii secretes compounds that mimic bacterial signals and interfere with quorum sensing regulation in bacteria

Teplitski, Max; Chen, Hancai; Rajamani, S; Gao, Mengsheng; Merighi, M; Sayre, Richard T; Robinson, Jayne B; Rolfe, Barry; Bauer, Wolfgang

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The unicellular soil-freshwater alga Chlamydomonas reinhardtii was found to secrete substances that mimic the activity of the N-acyl-L-homoserine lactone (AHL) signal molecules used by many bacteria for quorum sensing regulation of gene expression. More than a dozen chemically separable but unidentified substances capable of specifically stimulating the LasR or CepR but not the LuxR, AhyR, or CviR AHL bacterial quorum sensing reporter strains were detected in ethyl acetate extracts of C....[Show more]

dc.contributor.authorTeplitski, Max
dc.contributor.authorChen, Hancai
dc.contributor.authorRajamani, S
dc.contributor.authorGao, Mengsheng
dc.contributor.authorMerighi, M
dc.contributor.authorSayre, Richard T
dc.contributor.authorRobinson, Jayne B
dc.contributor.authorRolfe, Barry
dc.contributor.authorBauer, Wolfgang
dc.date.accessioned2015-12-13T23:10:05Z
dc.identifier.issn0032-0889
dc.identifier.urihttp://hdl.handle.net/1885/87289
dc.description.abstractThe unicellular soil-freshwater alga Chlamydomonas reinhardtii was found to secrete substances that mimic the activity of the N-acyl-L-homoserine lactone (AHL) signal molecules used by many bacteria for quorum sensing regulation of gene expression. More than a dozen chemically separable but unidentified substances capable of specifically stimulating the LasR or CepR but not the LuxR, AhyR, or CviR AHL bacterial quorum sensing reporter strains were detected in ethyl acetate extracts of C. reinhardtii culture filtrates. Colonies of C. reinhardtii and Chlorella spp. stimulated quorum sensing-dependent luminescence in Vibrio harveyi, indicating that these algae may produce compounds that affect the AI-2 furanosyl borate diester-mediated quorum sensing system of Vibrio spp. Treatment of the soil bacterium Sinorhizobium meliloti with a partially purified LasR mimic from C. reinhardtii affected the accumulation of 16 of the 25 proteins that were altered in response to the bacterium's own AHL signals, providing evidence that the algal mimic affected quorum sensing-regulated functions in this wild-type bacterium. Peptide mass fingerprinting identified 32 proteins affected by the bacterium's AHLs or the purified algal mimic, including GroEL chaperonins, the nitrogen regulatory protein PII, and a GTP-binding protein. The algal mimic was able to cancel the stimulatory effects of bacterial AHLs on the accumulation of seven of these proteins, providing evidence that the secretion of AHL mimics by the alga could be effective in disruption of quorum sensing in naturally encountered bacteria.
dc.publisherAmerican Society of Plant Biologists
dc.sourcePlant Physiology
dc.subjectKeywords: Bacteria; Genes; Luminescence; Physiology; Soils; Quorum sensing; Signal molecules; Algae; algal protein; bacterial protein; drug derivative; gamma butyrolactone; homoserine lactone; proteome; protozoal protein; animal; article; bacterial phenomena and fu
dc.titleChlamydomonas reinhardtii secretes compounds that mimic bacterial signals and interfere with quorum sensing regulation in bacteria
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume134
dc.date.issued2004
local.identifier.absfor060111 - Signal Transduction
local.identifier.ariespublicationMigratedxPub16514
local.type.statusPublished Version
local.contributor.affiliationTeplitski, Max, University of Florida
local.contributor.affiliationChen, Hancai, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationRajamani, S, Ohio State University
local.contributor.affiliationGao, Mengsheng, Ohio State University
local.contributor.affiliationMerighi, M, Ohio State University
local.contributor.affiliationSayre, Richard T, Ohio State University
local.contributor.affiliationRobinson, Jayne B, University of Dayton
local.contributor.affiliationRolfe, Barry, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBauer, Wolfgang, Ohio State University
local.description.embargo2037-12-31
local.bibliographicCitation.startpage137
local.bibliographicCitation.lastpage146
local.identifier.doi10.1104/pp.103.029918
dc.date.updated2015-12-12T08:22:18Z
local.identifier.scopusID2-s2.0-0842328855
CollectionsANU Research Publications

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