Publication: Characterization of the biosynthetic gene cluster for cryptic phthoxazolin a in streptomyces avermitilis
Issued Date
2018-01-01
Resource Type
ISSN
19326203
Other identifier(s)
2-s2.0-85040347904
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
PLoS ONE. Vol.13, No.1 (2018)
Suggested Citation
Dian Anggraini Suroto, Shigeru Kitani, Masayoshi Arai, Haruo Ikeda, Takuya Nihira Characterization of the biosynthetic gene cluster for cryptic phthoxazolin a in streptomyces avermitilis. PLoS ONE. Vol.13, No.1 (2018). doi:10.1371/journal.pone.0190973 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/44897
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Characterization of the biosynthetic gene cluster for cryptic phthoxazolin a in streptomyces avermitilis
Other Contributor(s)
Abstract
© 2018 Suroto et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Phthoxazolin A, an oxazole-containing polyketide, has a broad spectrum of anti-oomycete activity and herbicidal activity. We recently identified phthoxazolin A as a cryptic metabolite of Streptomyces avermitilis that produces the important anthelmintic agent avermectin. Even though genome data of S. avermitilis is publicly available, no plausible biosynthetic gene cluster for phthoxazolin A is apparent in the sequence data. Here, we identified and characterized the phthoxazolin A (ptx) biosynthetic gene cluster through genome sequencing, comparative genomic analysis, and gene disruption. Sequence analysis uncovered that the putative ptx biosynthetic genes are laid on an extra genomic region that is not found in the public database, and 8 open reading frames in the extra genomic region could be assigned roles in the biosynthesis of the oxazole ring, triene polyketide and carbamoyl moieties. Disruption of the ptxA gene encoding a discrete acyltransferase resulted in a complete loss of phthoxazolin A production, confirming that the trans-AT type I PKS system is responsible for the phthoxazolin A biosynthesis. Based on the predicted functional domains in the ptx assembly line, we propose the biosynthetic pathway of phthoxazolin A.