ArticleProceedings of the National Academy of Sciences of the United States of America2021
A [3Fe-4S] cluster and tRNA-dependent aminoacyltransferase BlsK in the biosynthesis of Blasticidin S.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Phage hijacks host phosphorothioate DNA modification machinery to circumvent bacterial Ssp defences.Nature microbiology · 2026Article
- Blasticidin S Biosynthesis Involves a Unique Interplay between a Radical SAM Dehydratase, a Transaminase and an ATP-Grasp Ligase in Order to Avoid a Futile Cycle.ACS catalysis · 2025Article
- Mechanism of Catalysis and Substrate Binding of Epoxyqueuosine Reductase in the Biosynthetic Pathway to Queuosine-Modified tRNA.Biochemistry · 2025Article
- Intracellularly driven chemical modifications of antimicrobial secondary metabolites: Potent mechanisms of self-resistance.Pharmaceutical science advances · 2024Review
- Research progress in the role and mechanism of Leucine in regulating animal growth and development.Frontiers in physiology · 2023Review
- RadicalJournal of the American Chemical Society · 2022Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
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Abstract
Blasticidin S is a peptidyl nucleoside antibiotic. Its biosynthesis involves a cryptic leucylation and two leucylated intermediates, LDBS and LBS, have been found in previous studies. Leucylation has been proposed to be a new self-resistance mechanism during blasticidin S biosynthesis, and the leucyl group was found to be important for the methylation of β-amino group of the arginine side chain. However, the responsible enzyme and its associated mechanism of the leucyl transfer process remain to be elucidated. Here, we report results investigating the leucyl transfer step forming the intermediate LDBS in blasticidin biosynthesis. A hypothetical protein, BlsK, has been characterized by genetic and in vitro biochemical experiments. This enzyme catalyzes the leucyl transfer from leucyl-transfer RNA (leucyl-tRNA) to the β-amino group on the arginine side chain of DBS. Furthermore, BlsK was found to contain an iron-sulfur cluster that is necessary for activity. These findings provide an example of an iron-sulfur protein that catalyzes an aminoacyl-tRNA (aa-tRNA)-dependent amide bond formation in a natural product biosynthetic pathway.
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