ArticleNucleic acids research2017
A structural basis for the antibiotic resistance conferred by an N1-methylation of A1408 in 16S rRNA.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
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Who cites it
9 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.
- RNA Drugs and RNA Targets for Small Molecules: Principles, Progress, and Challenges.Pharmacological reviews · 2020Pooled it
- Basis for selective drug evasion of an aminoglycoside-resistance ribosomal RNA modification.Nature communications · 2025Article
- The diverse landscape of RNA modifications in cancer development and progression.Genes & genomics · 2025Review
- mRNA modifications in cardiovascular biology and disease: with a focus on m6A modification.Cardiovascular research · 2022Review
- Adaptation and Exaptation: From Small Molecules to Feathers.Journal of molecular evolution · 2022Article
- Review
- Aminoglycoside Resistance: Updates with a Focus on Acquired 16S Ribosomal RNA Methyltransferases.Infectious disease clinics of North America · 2020Review
- Methylation of Ribosomal RNA: A Mitochondrial Perspective.Frontiers in genetics · 2020Review
- Structural Bases for the Fitness Cost of the Antibiotic-Resistance and Lethal Mutations at Position 1408 of 16S rRNA.Molecules (Basel, Switzerland) · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aminoglycoside resistance conferred by an N1-methylation of A1408 in 16S rRNA by a novel plasmid-mediated methyltransferase NpmA can be a future health threat. In the present study, we have determined crystal structures of the bacterial ribosomal decoding A site with an A1408m1A antibiotic-resistance mutation both in the presence and absence of aminoglycosides. G418 and paromomycin both possessing a 6'-OH group specifically bind to the mutant A site and disturb its function as a molecular switch in the decoding process. On the other hand, binding of gentamicin with a 6'-NH3+ group to the mutant A site could not be observed in the present crystal structure. These observations agree with the minimum inhibitory concentration of aminoglycosides against Escherichia coli. In addition, one of our crystal structures suggests a possible conformational change of A1408 during the N1-methylation reaction by NpmA. The structural information obtained explains how bacteria acquire resistance against aminoglycosides along with a minimum of fitness cost by the N1-methylation of A1408 and provides novel information for designing the next-generation aminoglycoside.
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