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Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin.

ABSTRACT: The thiazolylpeptides are a family of >50 bactericidal antibiotics that block the initial steps of bacterial protein synthesis. Here, we report a biosynthetic gene cluster for thiocillin and establish that it, and by extension the whole class, is ribosomally synthesized. Remarkably, the C-terminal 14 residues of a 52-residue peptide precursor undergo 13 posttranslational modifications to give rise to thiocillin, making this antibiotic the most heavily posttranslationally-modified peptide known to date.

SUBMITTER: Wieland Brown LC

PROVIDER: S-EPMC2650375 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

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Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin.

Wieland Brown Laura C LC Acker Michael G MG Clardy Jon J Walsh Christopher T CT Fischbach Michael A MA

Proceedings of the National Academy of Sciences of the United States of America 20090205 8

The thiazolylpeptides are a family of >50 bactericidal antibiotics that block the initial steps of bacterial protein synthesis. Here, we report a biosynthetic gene cluster for thiocillin and establish that it, and by extension the whole class, is ribosomally synthesized. Remarkably, the C-terminal 14 residues of a 52-residue peptide precursor undergo 13 posttranslational modifications to give rise to thiocillin, making this antibiotic the most heavily posttranslationally-modified peptide known t ...[more]

PMID: 19196969

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