Biochemical analysis reveals functional substitution of penultimate threonine in lasso peptides, indicating its sidechain acts as a key recognition motif for processing machinery.
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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Pan et al. (2011) studied this question.
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