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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/44897
Title: Characterization of the biosynthetic gene cluster for cryptic phthoxazolin a in streptomyces avermitilis
Authors: Dian Anggraini Suroto
Shigeru Kitani
Masayoshi Arai
Haruo Ikeda
Takuya Nihira
Osaka University
Mahidol University
Kitasato University
Keywords: Agricultural and Biological Sciences;Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2018
Citation: PLoS ONE. Vol.13, No.1 (2018)
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85040347904&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/44897
ISSN: 19326203
Appears in Collections:Scopus 2018

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