PMID:24056099

Citation	Kimbrough, JH and Stabb, EV (2013) Substrate specificity and function of the pheromone receptor AinR in Vibrio fischeri ES114. J. Bacteriol. 195:5223-32
Abstract	Two distinct but interrelated pheromone-signaling systems, LuxI/LuxR and AinS/AinR, positively control bioluminescence in Vibrio fischeri. Although each system generates an acyl-homoserine lactone (AHL) signal, the protein sequences of LuxI/LuxR and AinS/AinR are unrelated. AinS and LuxI generate the pheromones N-octanoyl-AHL (C8-AHL) and N-3-oxo-hexanoyl-AHL (3OC6-AHL), respectively. LuxR is a transcriptional activator that responds to 3OC6-AHL, and to a lesser extent to C8-AHL. AinR is hypothesized to respond to C8-AHL and, based on homology to Vibrio harveyi LuxN, to mediate the repression of a Qrr regulatory RNA. However, a ΔainR mutation decreased luminescence, which was not predicted based on V. harveyi LuxN, raising the possibility of a distinct regulatory mechanism for AinR. Here we show that ainR can complement a luxN mutant, suggesting functional similarity. Moreover, in V. fischeri, we observed ainR-dependent repression of a Pqrr-lacZ transcriptional reporter in the presence of C8-AHL, consistent with its hypothesized regulatory role. The system appears quite sensitive, with a half-maximal effect on a Pqrr reporter at 140 pM C8-AHL. Several other AHLs with substituted and unsubstituted acyl chains between 6 and 10 carbons also displayed an AinR-dependent effect on Pqrr-lacZ; however, AHLs with acyl chains of four carbons or 12 or more carbons lacked activity. Interestingly, 3OC6-AHL also affected expression from the qrr promoter, but this effect was largely luxR dependent, indicating a previously unknown connection between these systems. Finally, we propose a preliminary explanation for the unexpected luminescence phenotype of the ΔainR mutant.
Links	PubMed PMC3811584 Online version:10.1128/JB.00913-13
Keywords	4-Butyrolactone/analogs & derivatives; 4-Butyrolactone/metabolism; Aliivibrio fischeri/metabolism; Aliivibrio fischeri/physiology; Artificial Gene Fusion; Bacterial Proteins/metabolism; Gene Expression Regulation, Bacterial; Genes, Reporter; Homoserine/analogs & derivatives; Homoserine/metabolism; Lactones/metabolism; Receptors, Pheromone/metabolism; Signal Transduction; Substrate Specificity; beta-Galactosidase/analysis; beta-Galactosidase/genetics
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
VIBF1:Q5E615		GO:0000160: phosphorelay signal transduction system	ECO:0000315:		P		A change in the AinR mutation decreased luminescence which indicates that there may be a distinct regulatory mechanism for AinR.	complete CACAO 9602
VIBF1:Q5E615		GO:0008218: bioluminescence	ECO:0000316:	UniProtKB:A7N6S2 UniProtKB:P0C5S6 UniProtKB:P54302	P		Fig. 2 shows that the ainR mutant has decreased luminescence. This decreased luminescence can be mediated with the addition of C8-AHL. This shows that ainR in V. fischeri acts almost identically to luxN in V. harveyi.	complete CACAO 11477

References

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