ArticleProceedings of the National Academy of Sciences of the United States of America2022
The context of the ribosome binding site in mRNAs defines specificity of action of kasugamycin, an inhibitor of translation initiation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. 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, 29 citations in OpenAlex.
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- Structural modification of oxazolidinone antibiotics alters nascent peptide stalling preference and peptide trajectory through the ribosome.bioRxiv : the preprint server for biology · 2026Article
- Translational coupling of neighboring genes in prokaryotes.Journal of bacteriology · 2025Review
- Sequence-specific trapping of EF-Tu/glycyl-tRNA complex on the ribosome by bottromycin.bioRxiv : the preprint server for biology · 2025Article
- The translation inhibitors kasugamycin, edeine and GE81112 target distinct steps during 30S initiation complex formation.Nature communications · 2025Article
- Two dynamic N-terminal regions are required for function in ribosomal RNA adenine dimethylase family members.RNA (New York, N.Y.) · 2025Article
- Girolline is a sequence context-selective modulator of eIF5A activity.Nature communications · 2025Article
- In Vitro Response of Two Strains ofJournal of fungi (Basel, Switzerland) · 2024Article
- Paenilamicins are context-specific translocation inhibitors of protein synthesis.Nature chemical biology · 2024Article
- Increased Motility inInternational journal of molecular sciences · 2024Article
- Enantioselective Total Syntheses of (+)-Kasugamycin and (+)-Kasuganobiosamine Highlighting a Sulfamate-TetheredOrganic letters · 2024Article
- Paenilamicins from the honey bee pathogenbioRxiv : the preprint server for biology · 2024Article
- Single-molecule tracking reveals the functional allocation, in vivo interactions, and spatial organization of universal transcription factor NusG.Molecular cell · 2024Article
- Sulfamate-Tethered Aza-Wacker Strategy for a Kasugamine Synthon.The Journal of organic chemistry · 2024Article
- Article
- Motif-ation matters.Nature chemical biology · 2023Article
- Phage Cocktail in Combination with Kasugamycin as a Potential Treatment for Fire Blight Caused byAntibiotics (Basel, Switzerland) · 2022Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Kasugamycin (KSG) is an aminoglycoside antibiotic widely used in agriculture and exhibits considerable medical potential. Previous studies suggested that KSG interferes with translation by blocking binding of canonical messenger RNA (mRNA) and initiator transfer tRNA (tRNA) to the small ribosomal subunit, thereby preventing initiation of protein synthesis. Here, by using genome-wide approaches, we show that KSG can interfere with translation even after the formation of the 70S initiation complex on mRNA, as the extent of KSG-mediated translation inhibition correlates with increased occupancy of start codons by 70S ribosomes. Even at saturating concentrations, KSG does not completely abolish translation, allowing for continuing expression of some
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