Abstract
Cacaoidin is produced by the strain Streptomyces cacaoi CA-170360 and represents the first member of the new lanthidin (class V lanthipeptides) RiPP family. In this work, we describe the complete identification, cloning and heterologous expression of the cacaoidin biosynthetic gene cluster, which shows unique RiPP genes whose functions were not predicted by any bioinformatic tool. We also describe that the cacaoidin pathway is restricted to strains of the subspecies Streptomyces cacaoi subsp. cacaoi found in public genome databases, where we have also identified the presence of other putative class V lanthipeptide pathways. This is the first report on the heterologous production of a class V lanthipeptide.
Highlights
Actinomycetes are an extremely diverse group of Gram-positive, filamentous bacteria with high GC content genomes [1] considered as one of the most prolific sources for the discovery of new natural products (NPs) [2,3]
We describe the complete identification, cloning and heterologous expression of the cacaoidin biosynthetic gene cluster, which shows unique Ribosomally synthesized and Post-translationally modified Peptides (RiPPs) genes whose functions were not predicted by any bioinformatic tool
We describe that the cacaoidin pathway is restricted to strains of the subspecies Streptomyces cacaoi subsp. cacaoi found in public genome databases, where we have identified the presence of other putative class V lanthipeptide pathways
Summary
Actinomycetes are an extremely diverse group of Gram-positive, filamentous bacteria with high GC content genomes [1] considered as one of the most prolific sources for the discovery of new natural products (NPs) [2,3]. The genus Streptomyces produces over 70–80% of the secondary metabolites with described therapeutic properties [4]. The increasing number of sequenced genomes has revealed that actinomycetes carry the genetic potential to produce many more secondary metabolites than those detected under laboratory conditions [5]. Synthesized and Post-translationally modified Peptides (RiPPs) show more structural diversity than initially predicted from genome sequences [10]. Most RiPPs are synthesized as a longer precursor peptide, containing a C-terminal core peptide that undergoes a broad diversity of Post-Translational Modifications (PTMs) directed by the N-terminal leader peptide [11]
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