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Paromomycin binding induces a local conformational change in the A-site of 16 S rRNA

D Fourmy1, S Yoshizawa, J D Puglisi

  • 1Center for Molecular Biology of RNA, University of California, Santa Cruz, CA 95064, USA.

Insights

Aminoglycoside antibiotics disrupt bacterial translation by binding to ribosomal RNA. This study reveals how antibiotic binding alters RNA structure, affecting key residues and suggesting a mechanism for their action.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Aminoglycoside antibiotics target the ribosomal A-site RNA, causing genetic code misreading and inhibiting protein synthesis.
  • Previous studies determined the structure of the RNA-paromomycin complex using NMR spectroscopy.

Purpose of the Study:

  • To determine the free form structure of the A-site RNA using heteronuclear NMR.
  • To compare the free RNA structure with the paromomycin-bound structure.
  • To elucidate the conformational changes induced by aminoglycoside binding.

Main Methods:

  • Heteronuclear Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the structure of the free A-site RNA.
  • Comparative structural analysis was performed between the free and paromomycin-bound RNA forms.

Main Results:

  • The free A-site RNA structure was determined, revealing specific base-pairing interactions.
  • Comparison with the paromomycin-bound structure showed that conserved residues A1492 and A1493 are displaced towards the minor groove upon antibiotic binding.
  • These conformational changes position key nitrogen atoms (N1) of A1492 and A1493 on the minor groove side.

Conclusions:

  • The study reveals significant conformational changes in the A-site RNA upon aminoglycoside binding.
  • The displacement of A1492 and A1493 and their altered positioning suggest a direct role in the mechanism of aminoglycoside action.
  • These findings provide insights into how aminoglycosides interfere with bacterial translation.

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