Abstract:
:Aminoglycosides antibiotics negate dissociation and recycling of the bacterial ribosome's subunits by binding to Helix 69 (H69) of 23S rRNA. The differential binding of various aminoglycosides to the chemically synthesized terminal domains of the Escherichia coli and human H69 has been characterized using spectroscopy, calorimetry and NMR. The unmodified E. coli H69 hairpin exhibited a significantly higher affinity for neomycin B and tobramycin than for paromomycin (K(d)s = 0.3 +/- 0.1, 0.2 +/- 0.2 and 5.4 +/- 1.1 microM, respectively). The binding of streptomycin was too weak to assess. In contrast to the E. coli H69, the human 28S rRNA H69 had a considerable decrease in affinity for the antibiotics, an important validation of the bacterial target. The three conserved pseudouridine modifications (Psi1911, Psi1915, Psi1917) occurring in the loop of the E. coli H69 affected the dissociation constant, but not the stoichiometry for the binding of paromomycin (K(d) = 2.6 +/- 0.1 microM). G1906 and G1921, observed by NMR spectrometry, figured predominantly in the aminoglycoside binding to H69. The higher affinity of the E. coli H69 for neomycin B and tobramycin, as compared to paromomycin and streptomycin, indicates differences in the efficacy of the aminoglycosides.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Scheunemann AE,Graham WD,Vendeix FA,Agris PFdoi
10.1093/nar/gkp1253subject
Has Abstractpub_date
2010-05-01 00:00:00pages
3094-105issue
9eissn
0305-1048issn
1362-4962pii
gkp1253journal_volume
38pub_type
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