Ribosomal peptides with polycyclic isoprenoid moieties.

ABSTRACT: Isoprenoid modifications of proteins and peptides serve fundamental biological functions and are of therapeutic interest. While C₁₅ (farnesyl) and C₂₀ (geranylgeranyl) moieties are prevalent among proteins, known ribosomal peptide prenylations involve shorter-chain units not exceeding farnesyl in size. To our knowledge, cyclized terpene moieties have not been reported from either biomolecule class. Here we used targeted genome mining and heterologous pathway reconstitution to identify ribosomally synthesized and post-translationally modified peptides (RiPPs) with elaborate, cyclized geranylgeranyl modifications. The installing maturases commonly feature fused prenyltransferase-terpene cyclase architectures. We characterized two bifunctional maturases with distinct pre

SUBMITTER: Hubrich F 

PROVIDER: S-EPMC11484575 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature