Characterization of Leader Processing Shows That Partially Processed Mersacidin Is Activated by AprE After Export.

ABSTRACT: The ribosomally synthesized and post-translationally modified peptide mersacidin is a class II lanthipeptide with good activity against Gram-positive bacteria. The intramolecular lanthionine rings, that give mersacidin its stability and antimicrobial activity, are specific structures with potential applications in synthetic biology. To add the mersacidin modification enzymes to the synthetic biology toolbox, a heterologous expression system for mersacidin in Escherichia coli has recently been developed. While this system was able to produce fully modified mersacidin precursor peptide that could be activated by Bacillus amyloliquefaciens supernatant and showed that mersacidin was activated in an additional proteolytic step after transportation out of the cell, it lacked a mech

SUBMITTER: Viel JH 

PROVIDER: S-EPMC8581636 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature