Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM

• Wen Li ^[1] ; Xabier Agirrezabala ^[1] ; Jianlin Lei ^[1] ; Lamine Bouakaz ^[4] ; Julie L Brunelle ^[2] ; Rodrigo F Ortiz-Meoz ^[2] ; Rachel Green ^[2] ; Suparna Sanyal ^[3] ; Måns Ehrenberg ^[3] ; Joachim Frank ^[1]
  1. [1] Columbia University

     Columbia University

     Estados Unidos

     
  2. [2] Howard Hughes Medical Institute

     Howard Hughes Medical Institute

     Estados Unidos

     
  3. [3] Uppsala University

     Uppsala University

     Uppsala domkyrkoförs., Suecia

     
  4. [4] BioPharmaceutical Operations, Novartis Pharma AG, Basel, Switzerland

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• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 27, Nº. 24, 2008, págs. 3322-3331
• Idioma: inglés
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• Resumen

  • The accuracy of ribosomal translation is achieved by an initial selection and a proofreading step, mediated by EF-Tu, which forms a ternary complex with aminoacyl(aa)-tRNA. To study the binding modes of different aa-tRNAs, we compared cryo-EM maps of the kirromycin-stalled ribosome bound with ternary complexes containing Phe-tRNAPhe, Trp-tRNATrp, or Leu-tRNALeuI. The three maps suggest a common binding manner of cognate aa-tRNAs in their specific binding with both the ribosome and EF-Tu. All three aa-tRNAs have the same ‘loaded spring' conformation with a kink and twist between the D-stem and anticodon stem. The three complexes are similarly integrated in an interaction network, extending from the anticodon loop through h44 and protein S12 to the EF-Tu-binding CCA end of aa-tRNA, proposed to signal cognate codon–anticodon interaction to the GTPase centre and tune the accuracy of aa-tRNA selection.