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Ryan, K. S. 2011: Biosynthetic gene cluster for the cladoniamides, bis-indoles with a rearranged scaffold. - PLoS ONE 6(8): . [RLL List # 233 / Rec.# 35084]
Keywords: alkaloid/ alpha beta hydrolase/ carbazole derivative/ cladoniamide/ hydrolase/ indolocarbazole/ methyltransferase/ molecular scaffold/ oxygenase/ quercetin/ tryptophan/ unclassified drug/ bacterial protein/ carboline derivative/ indole derivative/ rebeccamycin/ tryptoline/ article/ bioaccumulation/ biosynthesis/ controlled study/ dimerization/ enzyme structure/ enzyme substrate complex/ gene cluster/ gene rearrangement/ genetic organization/ genetic similarity/ molecular interaction/ nucleotide sequence/ sequence homology/ bacterial gene/ biosynthesis/ chemistry/ enzymology/ genetics/ metabolism/ molecular genetics/ multigene family/ Streptomyces/ Streptomyces/ Alkaloids/ Bacterial Proteins/ Biosynthetic Pathways/ Carbazoles/ Carbolines/ Genes, Bacterial/ Indoles/ Molecular Sequence Data/ Multigene Family/ Streptomyces
Abstract: The cladoniamides are bis-indole alkaloids isolated from Streptomyces uncialis, a lichen-associated actinomycete strain. The cladoniamides have an unusual, indenotryptoline structure rarely observed among bis-indole alkaloids. I report here the isolation, sequencing, and annotation of the cladoniamide biosynthetic gene cluster and compare it to the recently published gene cluster for BE-54017, a closely related indenotryptoline natural product. The cladoniamide gene cluster differs from the BE-54017 gene cluster in gene organization and in the absence of one N-methyltransferase gene but otherwise contains close homologs to all genes in the BE-54017 cluster. Both gene clusters encode enzymes needed for the construction of an indolocarbazole core, as well as flavin-dependent enzymes putatively involved in generating the indenotryptoline scaffold from an indolocarbazole. These two bis-indolic gene clusters exemplify the diversity of biosynthetic routes that begin from the oxidative dimerization of two molecules of L-tryptophan, highlight enzymes for further study, and provide new opportunities for combinatorial engineering. © 2011 Katherine S. Ryan.

URL: http://dx.doi.org/10.1371/journal.pone.0023694

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