ArticleNature communications2024
Disordered regions in proteusin peptides guide post-translational modification by a flavin-dependent RiPP brominase.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Exploring Disordered Regions of Human Spliceosome Proteins.The journal of physical chemistry letters · 2026Article
- Myxarylin: TotalJournal of the American Chemical Society · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Stable association of a chlamydial symbiont with the freshwater predator hydra suggests broad host potential.The ISME journal · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Leader-Independent C‑Terminal Modification by a RadicalACS bio & med chem Au · 2025Article
- Peptide Prenylation Follows Divergent Substrate Engagement Rules.Journal of the American Chemical Society · 2025Article
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Large protein-like leader peptides engage differently with RiPP halogenases and lanthionine synthetases.Nature communications · 2025Article
- Peptidic Tryptophan Halogenation by a Promiscuous Flavin-Dependent Enzyme.Angewandte Chemie (International ed. in English) · 2025Article
- Extending the Peptide/Protein Interaction Paradigm to a Protein/Protein Engagement Model in RiPP Biosynthesis.ACS chemical biology · 2025Article
- Combatting virulent gut bacteria by inhibiting the biosynthesis of a two-component lanthipeptide toxin.Nature communications · 2025Article
- BeStSel: analysis site for protein CD spectra-2025 update.Nucleic acids research · 2025Article
- Transformation-Guided Genome Mining Provides Access to Brominated Lanthipeptides.Organic letters · 2025Article
- Genome mining for the discovery of peptide halogenases and their biochemical characterization.Methods in enzymology · 2025Article
- Peptide halogenation biochemistry: interfacing pharmaceutical deliverables with chemical innovation.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2025Review
- Halogenase-Assisted Alkyne/Aryl Bromide Sonogashira Coupling for Ribosomally Synthesized Peptides.Journal of the American Chemical Society · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
To biosynthesize ribosomally synthesized and post-translationally modified peptides (RiPPs), enzymes recognize and bind to the N-terminal leader region of substrate peptides which enables catalytic modification of the C-terminal core. Our current understanding of RiPP leaders is that they are short and largely unstructured. Proteusins are RiPP precursor peptides that defy this characterization as they possess unusually long leaders. Proteusin peptides have not been structurally characterized, and we possess scant understanding of how these atypical leaders engage with modifying enzymes. Here, we determine the structure of a proteusin peptide which shows that unlike other RiPP leaders, proteusin leaders are preorganized into a rigidly structured region and a smaller intrinsically disordered region. With residue level resolution gained from NMR titration experiments, the intermolecular peptide-protein interactions between proteusin leaders and a flavin-dependent brominase are mapped onto the disordered region, leaving the rigidly structured region of the proteusin leader to be functionally dispensable. Spectroscopic observations are biochemically validated to identify a binding motif in proteusin peptides that is conserved among other RiPP leaders as well. This study provides a structural characterization of the proteusin peptides and extends the paradigm of RiPP modification enzymes using not only unstructured peptides, but also structured proteins as substrates.
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