ArticleJournal of industrial microbiology & biotechnology2019
Investigations into PoyH, a promiscuous protease from polytheonamide biosynthesis.
Article in Journal of industrial microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Heterologously expressed SacP23, a novel bacteriocin fromRoyal Society open science · 2023Article
- RiPP enzyme heterocomplex structure-guided discovery of a bacterial borosin α-RSC chemical biology · 2023Article
- Marine Bacterial Ribosomal Peptides: Recent Genomics- and Synthetic Biology-Based Discoveries and Biosynthetic Studies.Marine drugs · 2022Review
- Understanding thioamitide biosynthesis using pathway engineering and untargeted metabolomics.Chemical science · 2021Article
- Recent Advances and Perspectives on Expanding the Chemical Diversity of Lasso Peptides.Frontiers in bioengineering and biotechnology · 2021Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Genome mining- and synthetic biology-enabled production of hypermodified peptides.Nature chemistry · 2019Article
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Authors and funding
3 authors.
Funding
Abstract
Polytheonamides are the most extensively modified ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) currently known. In RiPP biosynthesis, the processed peptide is usually released from a larger precursor by proteolytic cleavage to generate the bioactive terminal product of the pathway. For polytheonamides, which are members of a new RiPP family termed proteusins, we have recently shown that such cleavage is catalyzed by the cysteine protease PoyH acting on the precursor PoyA, both encoded in the polytheonamide biosynthetic gene cluster. We now report activity for PoyH under a variety of reaction conditions for different maturation states of PoyA and demonstrate a potential use of PoyH as a promiscuous protease to liberate and characterize RiPPs from other pathways. As a proof of concept, the identified recognition motif was introduced into precursors of the thiopeptide thiocillin and the lanthipeptide lichenicidin VK1, allowing for their site-specific cleavage with PoyH. Additionally, we show that PoyH cleavage is inhibited by PoyG, a previously uncharacterized chagasin-like protease inhibitor encoded in the polytheonamide gene cluster.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.