Functional Analysis of A Pyoverdine Synthetase from<i>Pseudomonas</i>sp. MIS38

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  • LIM Siew Ping
    Division of Biosphere Science, Graduate School of Environmental Science, Hokkaido University
  • ROONGSAWANG Niran
    Division of Biosphere Science, Graduate School of Environmental Science, Hokkaido University
  • WASHIO Kenji
    Division of Biosphere Science, Graduate School of Environmental Science, Hokkaido University
  • MORIKAWA Masaaki
    Division of Biosphere Science, Graduate School of Environmental Science, Hokkaido University

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  • Functional Analysis of A Pyoverdine Synthetase from Pseudomonas sp. MIS38

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Fluorescent Pseudomonas sp. MIS38 produces a cyclic lipopeptide, arthrofactin. Arthrofactin is synthesized by a unique nonribosomal peptide synthetase (NRPS) with dual C/E-domains. In this study, another class of cyclic peptide, pyoverdine, was isolated from MIS38, viz., Pvd38. The main fraction of Pvd38 had an m⁄z value of 1,064.57 and contained Ala, Glu, Gly, (OHOrn), Ser, and Thr at a ratio of 2:1:1:(1):1:1 in the peptide part, suggesting a new structure compound. A gene encoding NRPS for the chromophore part of Pvd38 was identified, and we found that it contained a conventional E-domain. Gene disruption completely impaired the production of Pvd38, demonstrating that the synthetase is functional. This observation allows us to conclude that different NRPS systems with dual C/E-domains (in arthrofactin synthetase) and a conventional E-domain (in pyoverdine synthetase) are both functional in MIS38.

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