Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
2008 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 27, no 24, 3322-3331 p.Article in journal (Refereed) Published
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-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI). 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.
Place, publisher, year, edition, pages
2008. Vol. 27, no 24, 3322-3331 p.
cryo-EM, decoding, EF-Tu, ribosome
Research subject Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-104041DOI: 10.1038/emboj.2008.243ISI: 000261785900010PubMedID: 19020518OAI: oai:DiVA.org:uu-104041DiVA: diva2:219279