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Title 

N-acylhomoserine lactonase-producing Rhodococcus spp. with different AHL-degrading activities

Authors 

S Y ParkB J HwangM H ShinJ A KimH K KimJung-Kee Lee

Publisher 

Wiley-Blackwell

Issue Date 

2006

Citation 

FEMS Microbiology Letters, vol. 261, no. 1, pp. 102-108

Keywords 

N-acylhomoserine lactonase (AHLase)quorum quenchingrhodococcus sp.bacterial enzymelactonelactone derivativen 3 oxohexanoylhomoserine lactonen acylhomoserine lactonasen acylhomoserine lactonen acylhomoserine lactone acylase

Abstract 

N-acylhomoserine lactones (AHLs) are conserved signal molecules that control diverse biological activities in quorum sensing system of Gram-negative bacteria. Recently, several soil bacteria were found to degrade AHLs, thereby interfering with the quorum sensing system. Previously, Rhodococcus erythropolis W2 was reported to degrade AHLs by both oxido-reductase and AHL-acylase. In the present study, two AHL-utilizing bacteria, strains LS31 and PI33, were isolated and identified as the genus Rhodococcus. They exhibited different AHL-utilization abilities: Rhodococcus sp. strain LS31 rapidly degraded a wide range of AHLs, including N-3-oxo-hexanoyl-L-homoserine lactone (OHHL), whereas Rhodococcus sp. strain PI33 showed relatively less activity towards 3-oxo substituents. Coculture of strain LS31 with Erwinia carotovora effectively reduced the amount of OHHL and pectate lyase activity, compared with coculture of strain PI33 with E. carotovora. A mass spectrometry analysis indicated that both strains hydrolyzed the lactone ring of AHL to generate acylhomoserine, suggesting that AHL-lactonases (AHLases) from the two Rhodococcus strains are involved in the degradation of AHL, in contrast to R. erythropolis W2. To the best of our knowledge, this is the first report on AHLases of Rhodococcus spp.

ISSN 

0378-1097

Link 

http://dx.doi.org/10.1111/j.1574-6968.2006.00336.x

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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