scholarly journals Elevated Temperature Enhances Short to Medium Chain Acyl Homoserine Lactone Production by Black Band Disease Associated Vibrios

2017 ◽  
pp. fix005 ◽  
Author(s):  
Chinmayee D. Bhedi ◽  
Carson W. Prevatte ◽  
Maggie S. Lookadoo ◽  
Patricia A. Waikel ◽  
Patrick M. Gillevet ◽  
...  
Keyword(s):  
Elevated Temperature ◽  
Homoserine Lactone ◽  
Acyl Homoserine Lactone ◽  
Black Band Disease ◽  
Medium Chain ◽  
Chain Acyl ◽  
Black Band

scholarly journals Long-Chain Acyl-Homoserine Lactone Quorum-Sensing Regulation of Rhodobacter capsulatus Gene Transfer Agent Production

2002 ◽  
Vol 184 (23) ◽  
pp. 6515-6521 ◽  
Author(s):  
Amy L. Schaefer ◽  
Terumi A. Taylor ◽  
J. Thomas Beatty ◽  
E. P. Greenberg
Keyword(s):  
Gene Transfer ◽  
Quorum Sensing ◽  
Rhodobacter Capsulatus ◽  
Homoserine Lactone ◽  
Acyl Homoserine Lactone ◽  
Homoserine Lactones ◽  
Acyl Homoserine Lactones ◽  
Chain Acyl ◽  
Gene Transfer Agent ◽  
Long Chain

ABSTRACT 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.

scholarly journals Identification of QuiP, the Product of Gene PA1032, as the Second Acyl-Homoserine Lactone Acylase of Pseudomonas aeruginosa PAO1

2006 ◽  
Vol 72 (2) ◽  
pp. 1190-1197 ◽  
Author(s):  
Jean J. Huang ◽  
Ashley Petersen ◽  
Marvin Whiteley ◽  
Jared R. Leadbetter
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Expression Patterns ◽  
Constitutive Expression ◽  
Homoserine Lactone ◽  
Growth Defect ◽  
Acyl Homoserine Lactone ◽  
Gene Encoding ◽  
Chain Acyl ◽  
Dependent Growth ◽  
Long Chain

ABSTRACT The relevance of the acyl homoserine lactone (acyl-HSL) quorum signals N-3-oxododecanoyl-homoserine lactone (3OC12HSL) and N-butanoyl-homoserine lactone to the biology and virulence of Pseudomonas aeruginosa is well investigated. Previously, P. aeruginosa was shown to degrade long-chain, but not short-chain, acyl-HSLs as sole carbon and energy sources (J. J. Huang, J.-I. Han, L.-H. Zhang, and J. R. Leadbetter, Appl. Environ. Microbiol. 69:5941-5949, 2003). A gene encoding an enzyme with acyl-HSL acylase activity, pvdQ (PA2385), was identified, but it was not required for acyl-HSL utilization. This indicated that P. aeruginosa encodes another acyl-HSL acylase, which we identify here. A comparison of total cell proteins of cultures grown with long-acyl acyl-HSLs versus other substrates implicated the involvement of a homolog of PvdQ, the product of gene PA1032, for which we propose the name QuiP. Transposon mutants of quiP were defective for growth when P. aeruginosa was cultured in medium containing decanoyl-HSL as a sole carbon and energy source. Complementation with a functional copy of quiP rescued this growth defect. When P. aeruginosa was grown in buffered lysogeny broth, constitutive expression of QuiP in P. aeruginosa led to decreased accumulations of the quorum signal 3OC12HSL, relative to the wild type. Heterologous expression of QuiP was sufficient to confer long-chain acyl-HSL acylase activity upon Escherichia coli. Examination of gene expression patterns during acyl-HSL-dependent growth of P. aeruginosa further supported the involvement of quiP in signal decay and revealed other genes also possibly involved. It is not yet known under which “natural” conditions quiP is expressed or how P. aeruginosa balances the expression of its quorum-sensing systems with the expression of its acyl-HSL acylase activities.

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