Work

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

Year: 2009

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.0900008106

Authors: Laura C. Wieland Brown, Michael G. Acker, Jon Clardy, Christopher T. Walsh, Michael A Fischbach

Institutions: Harvard University, Massachusetts General Hospital

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Applied Microbiology and Biotechnology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funders: National Cancer Institute, National Institute of General Medical Sciences