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Nonribosomal Peptide Synthesis in Animals: The Cyclodipeptide Synthase of Nematostella

2011; Elsevier BV; Volume: 18; Issue: 11 Linguagem: Inglês

10.1016/j.chembiol.2011.09.010

1879-1301

Jérôme Seguin, Mireille Moutiez, Yan Li, Pascal Belin, Alain Lecoq, Matthieu Fonvielle, Jean‐Baptiste Charbonnier, Jean‐Luc Pernodet, Muriel Gondry,

Carbohydrate Chemistry and Synthesis

Cyclodipeptide synthases (CDPSs) are small enzymes structurally related to class-I aminoacyl-tRNA synthetases (aaRSs). They divert aminoacylated tRNAs from their canonical role in ribosomal protein synthesis, for cyclodipeptide formation. All the CDPSs experimentally characterized to date are bacterial. We show here that a predicted CDPS from the sea anemone Nematostella vectensis is an active CDPS catalyzing the formation of various cyclodipeptides, preferentially containing tryptophan. Our findings demonstrate that eukaryotes encode active CDPSs and suggest that all CDPSs have a similar aminoacyl-tRNA synthetase-like architecture and ping-pong mechanism. They also raise questions about the biological roles of the cyclodipeptides produced in bacteria and eukaryotes.