The role of a conserved threonine residue in the leader peptide of lasso peptide precursors.
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.
Department of Chemical and Biological Engineering, A207 Engineering Quadrangle, Princeton University, Princeton, NJ 08544, USA.
Si Jia
SJ
Pan
Jakub
J
Rajniak
Mikhail O
MO
Maksimov
A James
AJ
Link
D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D017124:Conserved Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011498:Protein Precursors / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D013912:Threonine
D001430:Bacteriocins; D010455:Peptides; D011498:Protein Precursors; C533129:capistruin; C020411:microcin; D013912:Threonine