Detection and characterization of bacteria from the potato rhizosphere degrading N-acyl-homoserine lactone.
Quorum sensing plays a role in the regulation of soft rot diseases caused by the plant pathogenic bacterium Pectobacterium carotovorum subsp. carotovorum. The signal molecules involved in quorum sensing in P. carotovorum subsp. carotovorum belong to the group of N-acyl homoserine lactones (AHLs). In our study, we screened bacteria isolated from the potato rhizosphere for the ability to degrade AHLs produced by P. carotovorum subsp. carotovorum. Six isolates able to degrade AHLs were selected for further studies. According to 16S rDNA sequence analysis and fatty acid methyl ester profiling, the isolates belonged to the genera Ochrobactrum, Rhodococcus, Pseudomonas, Bacillus, and Delftia. For the genera Ochrobactrum and Delftia, for the first time AHL-degrading isolates were found. Data presented in this study revealed for the first time that Ochrobactrum sp. strain A44 showed the capacity to inactivate various synthetic AHL molecules; the substituted AHLs were inactivated with a lower efficiency than the unsubstituted AHLs. Compared with the other isolates, A44 was very effective in the degradation of AHLs produced by P. carotovorum subsp. carotovorum. It was verified by polymerase chain reaction, DNA-DNA hybridization, and a lactone ring reconstruction assay that Ochrobactrum sp. strain A44 did not possess AHL lactonase activity. AHL degradation in Ochrobactrum sp. strain A44 occurred intracellularly; it was not found in the culture supernatant. AHL-degrading activity of A44 was thermo sensitive. Experiments in planta revealed that Ochrobactrum sp. strain A44 significantly inhibited the maceration of potato tuber tissue. Since A44 did not produce antibiotics, the attenuation of the decay might be due to the quenching of quorum- sensing-regulated production of pectinolytic enzymes. The strain can potentially serve to control P. carotovorum subsp. carotovorum in potato.
Jafra
S
S
Plant Research International, Wageningen, Netherlands. jafra@biotech.univ.gda.pl
Przysowa
J
J
Czajkowski
R
R
Michta
A
A
Garbeva
P
P
van der Wolf
J M
JM
D015107:4-Butyrolactone / Q000031:analogs & derivatives* / Q000378:metabolism; D001407:Bacillus / Q000302:isolation & purification / Q000378:metabolism; D001419:Bacteria / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism*; D002265:Carboxylic Ester Hydrolases / Q000235:genetics; D004275:DNA, Ribosomal / Q000235:genetics; D042742:Delftia / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D042041:Ochrobactrum / Q000302:isolation & purification / Q000378:metabolism*; D016973:Pectobacterium carotovorum / Q000378:metabolism*; D053038:Quorum Sensing; D012336:RNA, Ribosomal, 16S / Q000235:genetics; D012240:Rhodococcus / Q000302:isolation & purification / Q000378:metabolism; D012988:Soil Microbiology; D011198:Solanum tuberosum / Q000382:microbiology*
D004275:DNA, Ribosomal; D012336:RNA, Ribosomal, 16S; C088386:homoserine lactone; D002265:Carboxylic Ester Hydrolases; C432003:N-acyl homoserine lactonase; D015107:4-Butyrolactone