The marine sponge Theonella swinhoei and its uncultivated bacterial endosymbionts are rich sources of bioactive secondary metabolites. Two of these metabolites, polytheonamides A and B, exhibit surprising structural complexity, with 13 of the 19 amino acids that constitute the 48-residue peptides being non-proteinogenic, leading to the general assumption that these peptides were synthesized by a non-ribosomal peptide synthase. However, by mining the sponge metagenome, Freeman et al. identified an operon, probably from a bacterial endosymbiont, that contains an ORF corresponding to an unprocessed polytheonamide precursor, supporting a ribosomal origin for these peptides. The operon also contains six candidate enzymes that probably carry out the 48 different post-translational modifications which help create the functional polytheonamides.
ORIGINAL RESEARCH PAPER
Freeman, M. F. et al. Metagenome mining reveals polytheonamides as posttranslationally modified ribosomal peptides. Science 338, 387–390 (2012)
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Jermy, A. Ribosomal origin for polytheonamides. Nat Rev Microbiol 10, 802 (2012). https://doi.org/10.1038/nrmicro2926
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DOI: https://doi.org/10.1038/nrmicro2926