N-acylhomoserine lactonase producing Rhodococcus spp. with different AHL-degrading activities.
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.
Park
Sun-Yang
SY
Systems Microbiology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Yuseung, Daejon, Korea.
Hwang
Byung-Joon
BJ
Shin
Min-Ho
MH
Kim
Jung-Ae
JA
Kim
Ha-Kun
HK
Lee
Jung-Kee
JK
D015107:4-Butyrolactone / Q000031:analogs & derivatives* / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism* / Q000502:physiology; D002244:Carbon / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism* / Q000502:physiology; D016973:Pectobacterium carotovorum / Q000378:metabolism; D012240:Rhodococcus / Q000145:classification / Q000201:enzymology* / Q000302:isolation & purification; D015398:Signal Transduction; D013379:Substrate Specificity
D001426:Bacterial Proteins; C088386:homoserine lactone; D002244:Carbon; D002265:Carboxylic Ester Hydrolases; C432003:N-acyl homoserine lactonase; D015107:4-Butyrolactone