Issue 13, 2012
From the journal:

Chemical Communications

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

Si Jia Pan,‡a   Jakub Rajniak,‡a   Mikhail O. Maksimova  and  A. James Link*ab  

* Corresponding authors

a Department of Chemical and Biological Engineering, A207 Engineering Quadrangle, Princeton University, Princeton, USA
E-mail: ajlink@princeton.edu
Tel: +1 609-258-7191

b Department of Molecular Biology, Princeton University, Princeton, USA

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

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Article information

DOI
https://doi.org/10.1039/C2CC17211A
Article type
Communication
Submitted
19 Nov 2011
Accepted
16 Dec 2011
First published
16 Dec 2011

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

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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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