Iterative glycosylation on a single residue of a mature lasso peptide.

ABSTRACT: Iterative catalysis is a unique characteristic of the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs) to boost structural and biological diversity. Lasso peptides are an abundant class of RiPPs featuring lariat knot structures, which pose obstacles to iterative post-translational modifications (PTMs) after macrocyclization. Here, we present a unique glycotransferase (GT), IgtG, that iteratively glycosylates a Ser residue up to four times within a mature lasso peptide, as the final biosynthetic step of davasins. Such iterative catalysis diverges from classical iterative modifications on linear peptides. Bioinformatic analysis reveals 24 IgtG-like GTs that are potentially involved in the biosynthesis of graspetides, and IgtG-like GTs are evolutionar

SUBMITTER: Sun K 

PROVIDER: S-EPMC11912497 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature