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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus cereus / genetics
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Chromatography, High Pressure Liquid
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Computational Biology
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Mass Spectrometry
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Molecular Sequence Data
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Multigene Family
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Mutagenesis, Insertional
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Oligopeptides / chemistry
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Oligopeptides / metabolism*
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Peptides / chemical synthesis*
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Peptides / genetics
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Peptides / pharmacology
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Protein Processing, Post-Translational*
Substances
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Oligopeptides
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Peptides
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thiocillin