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Journal of Bacteriology, December 2002, p. 6515-6521, Vol. 184, No. 23
0021-9193/02/$04.00+0 DOI: 10.1128/JB.184.23.6515-6521.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Terumi A. Taylor,2 J. Thomas Beatty,2 and E. P. Greenberg1*
Department of Microbiology and W. M. Keck Foundation Microbial Communities & Cell Signaling Laboratory, University of Iowa, Iowa City, Iowa 52242,1 Department of Microbiology & Immunology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z32
Received 29 May 2002/ Accepted 1 September 2002
Many proteobacteria use acyl-homoserine lactones as quorum-sensing signals. Traditionally, biological detection systems have been used to identify bacteria that produce acyl-homoserine lactones, although the specificities of these detection systems can limit discovery. We used a sensitive approach that did not require a bioassay to detect production of long-acyl-chain homoserine lactone production by Rhodobacter capsulatus and Paracoccus denitrificans. These long-chain acyl-homoserine lactones are not readily detected by standard bioassays. The most abundant acyl-homoserine lactone was N-hexadecanoyl-homoserine lactone. The long-chain acyl-homoserine lactones were concentrated in cells but were also found in the culture fluid. An R. capsulatus gene responsible for long-chain acyl-homoserine lactone synthesis was identified. A mutation in this gene, which we named gtaI, resulted in decreased production of the R. capsulatus gene transfer agent, and gene transfer agent production was restored by exogenous addition of N-hexadecanoyl-homoserine lactone. Thus, long-chain acyl-homoserine lactones serve as quorum-sensing signals to enhance genetic exchange in R. capsulatus.
Present address: W. M. Keck Microbial Communities & Cell Signaling Laboratory, Kewalo Marine Laboratories, Pacific Biomedical Research Center, University of Hawaii-Manoa, Honolulu, HI 96813.
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