Author:
Müller Christine,Birmes Franziska S.,Niewerth Heiko,Fetzner Susanne
Abstract
ABSTRACTA bacterial strain, which based on the sequences of its 16S rRNA,gyrB,catA, andqsdAgenes, was identified as aRhodococcussp. closely related toRhodococcus erythropolis, was isolated from soil by enrichment on thePseudomonasquinolone signal [PQS; 2-heptyl-3-hydroxy-4(1H)-quinolone], a quorum sensing signal employed by the opportunistic pathogenPseudomonas aeruginosa. The isolate, termedRhodococcussp. strain BG43, cometabolically degraded PQS and its biosynthetic precursor 2-heptyl-4(1H)-quinolone (HHQ) to anthranilic acid. HHQ degradation was accompanied by transient formation of PQS, and HHQ hydroxylation by cell extracts required NADH, indicating that strain BG43 has a HHQ monooxygenase isofunctional to the biosynthetic enzyme PqsH ofP. aeruginosa. The enzymes catalyzing HHQ hydroxylation and PQS degradation were inducible by PQS, suggesting a specific pathway. Remarkably,Rhodococcussp. BG43 is also capable of transforming 2-heptyl-4-hydroxyquinoline-N-oxide to PQS. It thus converts an antibacterial secondary metabolite ofP. aeruginosato a quorum sensing signal molecule.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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