ArticleACS synthetic biology2015
Recognition sequences and substrate evolution in cyanobactin biosynthesis.
Article in ACS synthetic biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 84 citations in OpenAlex.
- A Machine Learning-Based Genome Mining Approach Reveals Unprecedented Biarylitide Diversity.JACS Au · 2026Article
- Peptide Prenylation Follows Divergent Substrate Engagement Rules.Journal of the American Chemical Society · 2025Article
- Extending the Peptide/Protein Interaction Paradigm to a Protein/Protein Engagement Model in RiPP Biosynthesis.ACS chemical biology · 2025Article
- α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.Protein science : a publication of the Protein Society · 2025Article
- De novo design of ribosomally synthesized and post-translationally modified peptides.Nature chemistry · 2025Article
- Genome-informed Discovery of Monchicamides A-K: Cyanobactins from the Microcoleaceae Cyanobacterium LEGE 16532.Journal of natural products · 2025Article
- Disordered regions in proteusin peptides guide post-translational modification by a flavin-dependent RiPP brominase.Nature communications · 2024Article
- Systematic mining of the human microbiome identifies antimicrobial peptides with diverse activity spectra.Nature microbiology · 2023Article
- A Silent Biosynthetic Gene Cluster from a Methanotrophic Bacterium Potentiates Discovery of a Substrate Promiscuous Proteusin Cyclodehydratase.ACS chemical biology · 2022Article
- Control of Nucleophile Chemoselectivity in Cyanobactin YcaO Heterocyclases PatD and TruD.ACS chemical biology · 2022Article
- Article
- Discovery and characterisation of an amidine-containing ribosomally-synthesised peptide that is widely distributed in nature.Chemical science · 2021Article
- An Obligate Peptidyl Brominase Underlies the Discovery of Highly Distributed Biosynthetic Gene Clusters in Marine Sponge Microbiomes.Journal of the American Chemical Society · 2021Article
- Genome-Mining-Based Discovery of the Cyclic Peptide Tolypamide and TolF, a Ser/Thr Forward O-Prenyltransferase.Angewandte Chemie (International ed. in English) · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Recent advances in the biosynthesis of RiPPs from multicore-containing precursor peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Article
- Expanding the chemical space of synthetic cyclic peptides using a promiscuous macrocyclase from prenylagaramide biosynthesis.ACS catalysis · 2020Article
- Pagoamide A, a Cyclic Depsipeptide Isolated from a Cultured Marine Chlorophyte,Journal of natural products · 2020Article
- Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products are of broad interest because of their intrinsic bioactivities and potential for synthetic biology. The RiPP cyanobactin pathways pat and tru have been experimentally shown to be extremely tolerant of mutations. In nature, the pathways exhibit "substrate evolution", where enzymes remain constant while the substrates of those enzymes are hypervariable and readily evolvable. Here, we sought to determine the mechanism behind this promiscuity. Analysis of a series of different enzyme-substrate combinations from five different cyanobactin gene clusters, in addition to engineered substrates, led us to define short discrete recognition elements within substrates that are responsible for directing enzymes. We show that these recognition sequences (RSs) are portable and can be interchanged to control which functional groups are added to the final natural product. In addition to the previously assigned N- and C-terminal proteolysis RSs, here we assign the RS for heterocyclization modification. We show that substrate elements can be swapped in vivo leading to successful production of natural products in E. coli. The exchangeability of these elements holds promise in synthetic biology approaches to tailor peptide products in vivo and in vitro.
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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.