ArticleJournal of the American Chemical Society2013
A general method for fluorescent labeling of the N-termini of lanthipeptides and its application to visualize their cellular localization.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Review
- Trifunctional Saxitoxin Conjugates for Covalent Labeling of Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2023Article
- Synthesis of Fluorescent Lanthipeptide Cytolysin S Analogues by Late-Stage Sulfamidate Ring Opening.Organic letters · 2023Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Solid-phase fluorescent BODIPY-peptide synthesisChemical science · 2020Article
- CylA is a sequence-specific protease involved in toxin biosynthesis.Journal of industrial microbiology & biotechnology · 2019Article
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
- Insights into the Biosynthesis of Duramycin.Applied and environmental microbiology · 2017Article
- Recombinant thiopeptides containing noncanonical amino acids.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Plantazolicin is an ultra-narrow spectrum antibiotic that targets theACS infectious diseases · 2016Article
- Structural Characterization and Bioactivity Analysis of the Two-Component Lantibiotic Flv System from a Ruminant Bacterium.Cell chemical biology · 2016Article
- Lights, Camera, Action! Antimicrobial Peptide Mechanisms Imaged in Space and Time.Trends in microbiology · 2016Review
- Applications of the class II lanthipeptide protease LicP for sequence-specific, traceless peptide bond cleavage.Chemical science · 2015Article
- A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.Nature chemical biology · 2015Article
- Facile Removal of Leader Peptides from Lanthipeptides by Incorporation of a Hydroxy Acid.Journal of the American Chemical Society · 2015Article
- Visualizing attack of Escherichia coli by the antimicrobial peptide human defensin 5.Biochemistry · 2015Article
- Application of meta- and para-Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release.Current protocols in protein science · 2015Article
- De novo biosynthesis of terminal alkyne-labeled natural products.Nature chemical biology · 2015Article
- Substrate control in stereoselective lanthionine biosynthesis.Nature chemistry · 2015Article
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2 authors.
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Abstract
Labeling of natural products with biophysical probes has greatly contributed to investigations of their modes of action and has provided tools for visualization of their targets. A general challenge is the availability of a suitable functional group for chemoselective modification. We demonstrate here that an N-terminal ketone is readily introduced into various lanthipeptides by the generation of a cryptic N-terminal dehydro amino acid by the cognate biosynthetic enzymes. Spontaneous hydrolysis of the N-terminal enamines results in α-ketoamides that site-specifically react with an aminooxy-derivatized alkyne or fluorophore. The methodology was successfully applied to prochlorosins 1.7 and 2.8, as well as the lantibiotics lacticin 481, haloduracin α, and haloduracin β. The fluorescently modified lantibiotics were added to bacteria, and their cellular localization was visualized by confocal fluorescence microscopy. Lacticin 481 and haloduracin α localized predominantly at sites of new and old cell division as well as in punctate patterns along the long axis of rod-shaped bacilli, similar to the localization of lipid II. On the other hand, haloduracin β was localized nonspecifically in the absence of haloduracin α, but formed specific patterns when coadministered with haloduracin α. Using two-color labeling, colocalization of both components of the two-component lantibiotic haloduracin was demonstrated. These data with living cells supports a model in which the α component recognizes lipid II and then recruits the β-component.
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