PMID:9573148
| Citation |
Val, DL and Cronan, JE Jr (1998) In vivo evidence that S-adenosylmethionine and fatty acid synthesis intermediates are the substrates for the LuxI family of autoinducer synthases. J. Bacteriol. 180:2644-51 |
|---|---|
| Abstract |
Many gram-negative bacteria synthesize N-acyl homoserine lactone autoinducer molecules as quorum-sensing signals which act as cell density-dependent regulators of gene expression. We have investigated the in vivo source of the acyl chain and homoserine lactone components of the autoinducer synthesized by the LuxI homolog, TraI. In Escherichia coli, synthesis of N-(3-oxooctanoyl)homoserine lactone by TraI was unaffected in a fadD mutant blocked in beta-oxidative fatty acid degradation. Also, conditions known to induce the fad regulon did not increase autoinducer synthesis. In contrast, cerulenin and diazoborine, specific inhibitors of fatty acid synthesis, both blocked autoinducer synthesis even in a strain dependent on beta-oxidative fatty acid degradation for growth. These data provide the first in vivo evidence that the acyl chains in autoinducers synthesized by LuxI-family synthases are derived from acyl-acyl carrier protein substrates rather than acyl coenzyme A substrates. Also, we show that decreased levels of intracellular S-adenosylmethionine caused by expression of bacteriophage T3 S-adenosylmethionine hydrolase result in a marked reduction in autoinducer synthesis, thus providing direct in vivo evidence that the homoserine lactone ring of LuxI-family autoinducers is derived from S-adenosylmethionine. |
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| Keywords |
Bacterial Proteins/metabolism; DNA Helicases/metabolism; Enzyme Induction/genetics; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Fatty Acids/biosynthesis; Fatty Acids/metabolism; Homoserine/biosynthesis; Hydrolases/metabolism; Mutation; S-Adenosylmethionine/biosynthesis; S-Adenosylmethionine/metabolism; Substrate Specificity; Transcription Factors/metabolism |
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