ArticleNature communications2017
Biosynthesis of the nosiheptide indole side ring centers on a cryptic carrier protein NosJ.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Synthesis, anti-tumor evaluation, and mechanistic investigation of 3-indolylpyrazole phenoxyacetamide derivatives against chronic myeloid leukemia cells.Molecular diversity · 2026Article
- Discovery and Biosynthesis of Persiathiacins: Unusual Polyglycosylated Thiopeptides Active Against Multidrug Resistant Tuberculosis.ACS infectious diseases · 2024Article
- Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022Review
- Whole genome sequencing ofBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Thiopeptides: antibiotics with unique chemical structures and diverse biological activities.The Journal of antibiotics · 2021Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Minimal lactazole scaffold for in vitro thiopeptide bioengineering.Nature communications · 2020Article
- The hidden enzymology of bacterial natural product biosynthesis.Nature reviews. Chemistry · 2019Article
- Capturing Intermediates in the Reaction Catalyzed by NosN, a Class C Radical S-Adenosylmethionine Methylase Involved in the Biosynthesis of the Nosiheptide Side-Ring System.Journal of the American Chemical Society · 2019Article
- Using Peptide Mimics to Study the Biosynthesis of the Side-Ring System of Nosiheptide.Methods in enzymology · 2018Article
- NosN, a Radical S-Adenosylmethionine Methylase, Catalyzes Both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide.Journal of the American Chemical Society · 2017Article
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Authors and funding
14 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nosiheptide is a prototypal thiopeptide antibiotic, containing an indole side ring in addition to its thiopeptide-characteristic macrocylic scaffold. This indole ring is derived from 3-methyl-2-indolic acid (MIA), a product of the radical S-adenosylmethionine enzyme NosL, but how MIA is incorporated into nosiheptide biosynthesis remains to be investigated. Here we report functional dissection of a series of enzymes involved in nosiheptide biosynthesis. We show NosI activates MIA and transfers it to the phosphopantetheinyl arm of a carrier protein NosJ. NosN then acts on the NosJ-bound MIA and installs a methyl group on the indole C4, and the resulting dimethylindolyl moiety is released from NosJ by a hydrolase-like enzyme NosK. Surface plasmon resonance analysis show that the molecular complex of NosJ with NosN is much more stable than those with other enzymes, revealing an elegant biosynthetic strategy in which the reaction flux is controlled by protein-protein interactions with different binding affinities.Thiopeptides such as nosiheptide are clinically-interesting antimicrobial natural products. Here the authors show the functional dissection of a series of enzymes involved in nosiheptide biosynthesis, revealing a unique biosynthetic pathway that centers on a previously-unknown carrier protein.
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