Issue 13, 2012

The role of a conserved threonine residue in the leader peptide of lasso peptide precursors

Abstract

The conserved threonine (Thr) residue in the penultimate position of the leader peptide of lasso peptides microcin J25 and capistruin can be effectively replaced by several amino acids close in size and shape to Thr. These findings suggest a model for lasso peptide biosynthesis in which the Thr sidechain is a recognition element for the lasso peptide maturation machinery.

Graphical abstract: The role of a conserved threonine residue in the leader peptide of lasso peptide precursors

Supplementary files

Article information

Article type
Communication
Submitted
19 Nov 2011
Accepted
16 Dec 2011
First published
16 Dec 2011

Chem. Commun., 2012,48, 1880-1882

The role of a conserved threonine residue in the leader peptide of lasso peptide precursors

S. J. Pan, J. Rajniak, M. O. Maksimov and A. J. Link, Chem. Commun., 2012, 48, 1880 DOI: 10.1039/C2CC17211A

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