Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.

ABSTRACT: Ribosomally synthesized and post-translationally modified peptides (RiPPs) have received much attention in recent years because of their promising bioactivities and the portability of their biosynthetic pathways. Heterologous expression studies of RiPP biosynthetic enzymes identified by genome mining often leave a leader peptide on the final product to prevent toxicity to the host and to allow the attachment of a genetically encoded affinity purification tag. Removal of the leader peptide to produce the mature natural product is then carried out in vitro with either a commercial protease or a protease that fulfills this task in the producing organism. This review covers the advances in characterizing these latter cognate proteases from bacterial RiPPs and their utility as sequence-dependen

SUBMITTER: Eslami SM 

PROVIDER: S-EPMC10885120 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature