Browsing by Author "Hong, K."
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Item Draft genome sequence of Streptomyces sp. strain CT34, isolated from a Ghanaian soil sample(Genome Announcements, 2015-02) Zhai, Y.; Cheng, B.; Hu, J.; Kyeremeh, K.; Wang, X.; Jaspars, M.; Deng, H.; Deng, Z.-X.; Hong, K.Presented here is a draft genome sequence of Streptomyces sp. strain CT34, which produces a novel ribosomally synthesized and posttranslationally modified peptide (RiPP). Analysis of the deduced open reading frame set identified the putative RiPP biosynthesis gene cluster, as well as other secondary metabolite gene clusters. © 2015 Zhai et al.Item Legonaridin, a new member of linaridin RiPP from a Ghanaian Streptomyces isolate(Organic and Biomolecular Chemistry, 2015-10) Rateb, M.E.; Zhai, Y.; Ehrner, E.; Rath, C.M.; Wang, X.; Tabudravu, J.; Ebel, R.; Bibb, M.; Kyeremeh, K.; Dorrestein, P.C.; Hong, K.; Jaspars, M.; Deng, H.Linaridins are rare linear ribosomally-synthesized and post-translationally modified peptides (RiPPs) and only two, cypemycin and SGR-1832, in this family have been identified so far. Legonaridin 1 has been discovered as a new member of linaridins through chemical isolation, peptidogenomics, comprehensive 1- and 2-D NMR and advanced Marfey's analyses from the soil bacterium Streptomyces sp. CT34, an isolate collected from Legon, Ghana. Bioinformatics analysis of the gene cluster suggested that the biosynthesis of legonaridin 1 is different from those of cypemycin and SGR-1832. Consistent with bioinformatics and peptidogenomics analyses, 1 has a total of nine post-modifications, 8 dehydrobutyrine residues and a N,N-dimethylated N-terminus with a carboxylic acid at the C-terminus. Legonaridin 1 is structurally different from the two known linaridins comprising a new subfamily. This is the first time that NMR spectroscopy is used to establish the 2-D structure of a linaridin RiPP.