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

Huang, Jean J. and Petersen, Ashley and Whiteley, Marvin and Leadbetter, Jared R. (2006) Identification of QuiP, the Product of Gene PA1032, as the Second Acyl-Homoserine Lactone Acylase of Pseudomonas aeruginosa PAO1. Applied and Environmental Microbiology, 72 (2). pp. 1190-1197. ISSN 0099-2240. PMCID PMC1392938. doi:10.1128/AEM.72.2.1190-1197.2006.

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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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Leadbetter, Jared R.0000-0002-7033-0844
Additional Information:© 2006, American Society for Microbiology. Received 29 September 2005/ Accepted 14 November 2005 This research was supported by the W. M. Keck Foundation Fund for Discovery in Basic Medical Research at the California Institute of Technology, by the Powell Foundation, by EPA STAR Fellowship no. 91620301 (to J.J.H.), and by the Oklahoma Center for the Advancement of Science and Technology (to M.W.). We thank Gary Hathaway and the Peptide Facility at Caltech for peptide mass fingerprinting, Nathan Dalleska for technical discussions and help with performing LC/APCI-MS analyses, and our laboratory colleagues for their helpful comments. Supplemental material for this article may be found at
Funding AgencyGrant Number
W. M. Keck FoundationUNSPECIFIED
Chinese Academy of SciencesUNSPECIFIED
Environmental Protection Agency (EPA)91620301
Oklahoma Center for the Advancement of Science and TechnologyUNSPECIFIED
Issue or Number:2
PubMed Central ID:PMC1392938
Record Number:CaltechAUTHORS:HUAaem06
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ID Code:2708
Deposited By: Archive Administrator
Deposited On:21 Apr 2006
Last Modified:08 Nov 2021 19:50

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