Analysis of the cryptic biosynthetic gene cluster encoding the RiPP curacozole reveals a phenylalanine-specific peptide hydroxylase.

ABSTRACT: Curacozole is representative of a cyanobactin-like sub-family of ribosomally synthesized and post-translationally modified peptides (RiPPs). The molecule is distinguished by its small macrocyclic structure, a poly-azole sequence that includes a phenyloxazole moiety, and a d-allo-Ile residue. The enzymatic steps required for its formation are not well understood. The predicted biosynthetic gene cluster (BGC) for curacozole in Streptomyces curacoi is cryptic, but is shown to be potently activated upon constitutive expression of the bldA-specified Leu-tRNA(UUA) molecule. Heterologous expression and gene deletion studies have defined the minimum BGC as consisting of seven genes, czlA, D, E, B1, C1, F, and BC. The biosynthetic pathway is highly substrate tolerant, ac

SUBMITTER: Hollands S 

PROVIDER: S-EPMC11575548 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature