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

Si Jia Pan; Jakub Rajniak; Mikhail O Maksimov; A James Link

doi:10.1039/c2cc17211a

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

Chem Commun (Camb). 2012 Feb 11;48(13):1880-2. doi: 10.1039/c2cc17211a. Epub 2012 Jan 5.

Authors

Si Jia Pan¹, Jakub Rajniak, Mikhail O Maksimov, A James Link

Affiliation

¹ Department of Chemical and Biological Engineering, A207 Engineering Quadrangle, Princeton University, Princeton, NJ 08544, USA.

PMID: 22222556
DOI: 10.1039/c2cc17211a

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.

MeSH terms

Amino Acid Sequence
Bacteriocins / biosynthesis
Bacteriocins / chemistry*
Bacteriocins / metabolism
Conserved Sequence*
Models, Molecular
Molecular Sequence Data
Peptides / chemistry*
Peptides / metabolism
Protein Conformation
Protein Precursors / biosynthesis
Protein Precursors / chemistry*
Protein Precursors / metabolism
Threonine*

Substances

Bacteriocins
Peptides
Protein Precursors
capistruin
microcin
Threonine