Functional analysis of a pyoverdine synthetase from Pseudomonas sp. MIS38.
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.
Lim
Siew Ping
SP
Division of Biosphere Science, Graduate School of Environmental Science, Hokkaido University, Sapporo, Japan.
Roongsawang
Niran
N
Washio
Kenji
K
Morikawa
Masaaki
M
D009842:Oligopeptides / Q000096:biosynthesis*; D010453:Peptide Synthases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D010456:Peptides, Cyclic / Q000096:biosynthesis; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000201:enzymology*; D011551:Pseudomonas fluorescens / Q000201:enzymology
D009842:Oligopeptides; D010456:Peptides, Cyclic; C042453:pyoverdin; D010453:Peptide Synthases; C486863:arthrofactin synthetase; C104385:non-ribosomal peptide synthase