Open AccessDetection of nonribosomal peptide synthetase genes in Xylaria sp. BCC1067 and cloning of XyNRPSA
Author(s) -
Paungmoung Porntip,
Punya Jantira,
Pongpattanakitshote Somchai,
Jeamton Wattana,
Vichisoonthonkul Taweerat,
Bhumiratana Sakarindr,
Tanticharoen Morakot,
Linne Uwe,
Marahiel Mohamed A.,
Cheevadhanarak Supapon
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2007.00843.x
Subject(s) - nonribosomal peptide , biology , gene cluster , gene , biochemistry , metabolite , biosynthesis , homology (biology)
Nonribosomal peptides, synthesized by nonribosomal peptide synthetases (NRPS), are an important group of diverse bioactive fungal metabolites. Xylaria sp. BCC1067, which is known to produce a variety of biologically active metabolites, was studied for gene encoding NRPS by two different PCR‐based methods and seven different NRPS fragments were obtained. In addition, screening a genomic library with an amplified NRPS fragment as a probe identified a putative NRPS gene named XyNRPSA . The functionality of XyNRPSA for the production of a corresponding metabolite was probed by gene insertion inactivation. Comparing the disrupting metabolite profile with that of the wild type led to the identification of a speculated metabolite. The crude extract of Xylaria sp. BCC1067 also exhibits antifungal activity against the human pathogens Candida albicans and Trichophyton mentagrophytes . However, the evaluation of biological activity of the XyNRPSA product suggests that it is neither a compound with antifungal activity nor a siderophore. In the vicinity of XyNRPSA , a second gene (named XyPtB ) was identified. Its localization and homology to orfB of the ergot alkaloid biosynthetic gene cluster suggests that XyPtB may be involved in XyNRPSA product biosynthesis.