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Aminoglycoside binding displaces a divalent metal ion in a tRNA-neomycin B complex
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. (Kirsebom)
2001 (English)In: Nature Structural Biology, ISSN 1072-8368, Vol. 8, no 6, 510-514 p.Article in journal (Refereed) Published
Abstract [en]

Aminoglycosides bind to RNA and interfere with its function, and it has been suggested that aminoglycoside binding to RNA displaces essential divalent metal ions. Here we demonstrate that addition of various aminoglycosides inhibited Pb2+-induced cleavage of yeast tRNA(Phe). Cocrystallization of yeast tRNA(Phe) and an aminoglycoside, neomycin B, resulted in crystals that diffracted to 2.6 A and the structure of the complex was solved by molecular replacement. The structure shows that the neomycin B binding site overlaps with known divalent metal ion binding sites in yeast tRNA(Phe), providing direct evidence for the hypothesis that aminoglycosides displace metal ions. Additionally, the neomycin B binding site overlaps with major determinants for Escherichia coli phenylalanyl-tRNA-synthetase. Here we present data demonstrating that addition of neomycin B inhibited aminoacylation of E. coli tRNA(Phe) in the mid microM range. Given that aminoglycoside and metal ion binding sites overlap, we discuss that aminoglycosides can be considered as 'metal mimics'.

Place, publisher, year, edition, pages
2001. Vol. 8, no 6, 510-514 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-147833DOI: 10.1038/88569ISI: 000168924300013PubMedID: 11373618OAI: oai:DiVA.org:uu-147833DiVA: diva2:400920
Available from: 2011-02-28 Created: 2011-02-28 Last updated: 2017-12-11Bibliographically approved

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