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PMID: 10655610 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Conformational switch in the decoding region of 16S rRNA during aminoacyl-tRNA selection on the ribosome.

Nature structural biology ·Vol. 7 ·No. 2 ·2000-02-00 ·Pages 104-7

Pape T, Wintermeyer W, Rodnina MV

Abstract

Binding of aminoglycoside antibiotics to 16S ribosomal RNA induces a particular structure of the decoding center and increases the misincorporation of near-cognate amino acids. By kinetic analysis we show that this is due to stabilization of the near-cognate codon recognition complex and the acceleration of two rearrangements that limit the rate of amino acid incorporation. The same rearrangement steps are accelerated in the cognate coding situation. We suggest that cognate codon recognition, or near-cognate codon recognition augmented by aminoglycoside binding, promote the transition of 16S rRNA from a 'binding' to a 'productive' conformation that determines the fidelity of decoding.

MeSH Terms
Anti-Bacterial Agents/pharmacology Binding Sites Guanosine Triphosphate/metabolism Hydrolysis/drug effects Leucine/metabolism Nucleic Acid Conformation Paromomycin/pharmacology Peptide Elongation Factor Tu/metabolism Protein Biosynthesis/physiology RNA, Ribosomal, 16S/chemistry,drug effects,metabolism RNA, Transfer, Amino Acyl/metabolism RNA, Transfer, Phe/drug effects,metabolism Ribosomes/metabolism
Chemicals
Anti-Bacterial Agents RNA, Ribosomal, 16S RNA, Transfer, Amino Acyl RNA, Transfer, Phe Paromomycin Guanosine Triphosphate Peptide Elongation Factor Tu Leucine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pape T
Institute of Molecular Biology, University of Witten/Herdecke, 58448 Witten, Germany.
Wintermeyer W
Rodnina M V
Article Info
Journal
Nature structural biology
Abbr.
Nat Struct Biol
ISSN
1072-8368
Published
2000-02-00
Pages
104-7
Language
English
Region
United States
NLM ID
9421566
Subset
IM
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