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

Wen Li, Xabier Agirrezabala, Jianlin Lei, Lamine Bouakaz, Julie L. Brunelle, Rodrigo F. Ortiz-Meoz, Rachel Green, Suparna Sanyal, Måns Ehrenberg, Joachim Frank

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)3322-3331
Number of pages10
JournalEMBO Journal
Volume27
Issue number24
DOIs
StatePublished - Dec 17 2008

Keywords

  • Cryo-EM
  • Decoding
  • EF-Tu
  • Ribosome

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology

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