Maturation of McjA precursor peptide into active microcin MccJ25

Microcin J25 is a ribosomally synthesised 21-residue antimicrobial peptide produced by certain strains of enterobacteria, that adopts an extraordinary 'threaded lasso' structure. To date, the biosynthesis of this peptide is little understood. Here we report the in vitro maturation of the m...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2007-01, Vol.5 (16), p.2564-2566
Main Authors: Clarke, David J, Campopiano, Dominic J
Format: Article
Language:English
Subjects:
Bacteriocins - biosynthesis
Bacteriocins - chemistry
Escherichia coli - metabolism
Mass Spectrometry - methods
Peptides - chemistry
Peptides - metabolism
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Summary:Microcin J25 is a ribosomally synthesised 21-residue antimicrobial peptide produced by certain strains of enterobacteria, that adopts an extraordinary 'threaded lasso' structure. To date, the biosynthesis of this peptide is little understood. Here we report the in vitro maturation of the microcin precursor peptide into active microcin J25 for the first time. Furthermore, we show that the enzymes required for the posttranslational modification of this precursor peptide are associated with the bacterial inner membrane.
ISSN:1477-0520
1477-0539
DOI:10.1039/b708478a