Functional Analysis of A Pyoverdine Synthetase from Pseudomonas sp. MIS38
-
- 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
Bibliographic Information
- Other Title
-
- Functional Analysis of A Pyoverdine Synthetase from<i>Pseudomonas</i>sp. MIS38
Search this article
Abstract
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.
Journal
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 71 (8), 2002-2009, 2007
Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390001206479019520
-
- NII Article ID
- 10027517861
-
- NII Book ID
- AA10824164
-
- ISSN
- 13476947
- 09168451
-
- HANDLE
- 2115/29888
-
- NDL BIB ID
- 8887750
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed