Issue 16, 2007

Maturation of McjA precursor peptide into active microcin MccJ25

Abstract

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.

Graphical abstract: Maturation of McjA precursor peptide into active microcin MccJ25

Supplementary files

Article information

Article type
Communication
Submitted
05 Jun 2007
Accepted
27 Jun 2007
First published
11 Jul 2007

Org. Biomol. Chem., 2007,5, 2564-2566

Maturation of McjA precursor peptide into active microcin MccJ25

D. J. Clarke and D. J. Campopiano, Org. Biomol. Chem., 2007, 5, 2564 DOI: 10.1039/B708478A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements