<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Gao M</submitter><funding>NIGMS NIH HHS</funding><pagination>7931-44</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1291280</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>187(23)</volume><pubmed_abstract>Quorum sensing (QS) in Sinorhizobium meliloti, the N-fixing bacterial symbiont of Medicago host plants, involves at least half a dozen different N-acyl homoserine lactone (AHL) signals and perhaps an equal number of AHL receptors. The accumulation of 55 proteins was found to be dependent on SinI, the AHL synthase, and/or on ExpR, one of the AHL receptors. Gas chromatography-mass spectrometry and electrospray ionization tandem mass spectrometry identified 3-oxo-C(14)-homoserine lactone (3-oxo-C(14)-HSL), C(16)-HSL, 3-oxo-C(16)-HSL, C(16:1)-HSL, and 3-oxo-C(16:1)-HSL as the sinI-dependent AHL QS signals accumulated by the 8530 expR(+) strain under the conditions used for proteome analysis. The 8530 expR(+) strain secretes additional, unidentified QS-active compounds. Addition of 200 nM C(14)</pubmed_abstract><journal>Journal of bacteriology</journal><pubmed_title>sinI- and expR-dependent quorum sensing in Sinorhizobium meliloti.</pubmed_title><pmcid>PMC1291280</pmcid><funding_grant_id>R01 GM042893</funding_grant_id><pubmed_authors>Robinson JB</pubmed_authors><pubmed_authors>Gao M</pubmed_authors><pubmed_authors>Eberhard A</pubmed_authors><pubmed_authors>Gronquist MR</pubmed_authors><pubmed_authors>Chen H</pubmed_authors><pubmed_authors>Rolfe BG</pubmed_authors><pubmed_authors>Bauer WD</pubmed_authors></additional><is_claimable>false</is_claimable><name>sinI- and expR-dependent quorum sensing in Sinorhizobium meliloti.</name><description>Quorum sensing (QS) in Sinorhizobium meliloti, the N-fixing bacterial symbiont of Medicago host plants, involves at least half a dozen different N-acyl homoserine lactone (AHL) signals and perhaps an equal number of AHL receptors. The accumulation of 55 proteins was found to be dependent on SinI, the AHL synthase, and/or on ExpR, one of the AHL receptors. Gas chromatography-mass spectrometry and electrospray ionization tandem mass spectrometry identified 3-oxo-C(14)-homoserine lactone (3-oxo-C(14)-HSL), C(16)-HSL, 3-oxo-C(16)-HSL, C(16:1)-HSL, and 3-oxo-C(16:1)-HSL as the sinI-dependent AHL QS signals accumulated by the 8530 expR(+) strain under the conditions used for proteome analysis. The 8530 expR(+) strain secretes additional, unidentified QS-active compounds. Addition of 200 nM C(14)</description><dates><release>2005-01-01T00:00:00Z</release><publication>2005 Dec</publication><modification>2025-04-04T09:51:38.596Z</modification><creation>2025-02-19T04:02:07.515Z</creation></dates><accession>S-EPMC1291280</accession><cross_references><pubmed>16291666</pubmed><doi>10.1128/jb.187.23.7931-7944.2005</doi><doi>10.1128/JB.187.23.7931-7944.2005</doi></cross_references></HashMap>