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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
Chem. Commun., 2012,48, 1880-1882
DOI:
10.1039/C2CC17211A
Received
19 Nov 2011,
Accepted
16 Dec 2011
First published online
16 Dec 2011
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.
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