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Issue 13, 2012
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The role of a conserved threonine residue in the leader peptide of lasso peptide precursors

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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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Publication details

The article was received on 19 Nov 2011, accepted on 16 Dec 2011 and first published on 16 Dec 2011


Article type: Communication
DOI: 10.1039/C2CC17211A
Citation: 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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