FEBS Letters
Volume 584, Issue 2 , Pages 252-264, 21 January 2010

Deciphering synonymous codons in the three domains of life: Co-evolution with specific tRNA modification enzymes

Edited by Manuel Santos

  • Henri Grosjean

      Affiliations

    • Université Paris-Sud, CNRS, UMR8621, Institut de Génétique et de Microbiologie, Orsay F-91405, France
    • Corresponding Author InformationCorresponding author. Fax: +33 (0) 169154629.
  • ,
  • Valérie de Crécy-Lagard

      Affiliations

    • Department of Microbiology and Cell Science, University of Florida, P.O. Box 110700, Gainesville, FL 32611-0700, USA
    • Fax: +1 352 392 5922.
  • ,
  • Christian Marck

      Affiliations

    • Institut de Biologie et de Technologies de Saclay (iBiTec-S) Bât 144, CEA/Saclay, F-91191 Gif-sur-Yvette Cedex, France
    • Fax: +33 (0) 169084712.

Received 22 September 2009; received in revised form 11 November 2009; accepted 16 November 2009. published online 19 November 2009.

Abstract 

The strategies organisms use to decode synonymous codons in cytosolic protein synthesis are not uniform. The complete isoacceptor tRNA repertoire and the type of modified nucleoside found at the wobble position 34 of their anticodons were analyzed in all kingdoms of life. This led to the identification of four main decoding strategies that are diversely used in Bacteria, Archaea and Eukarya. Many of the modern tRNA modification enzymes acting at position 34 of tRNAs are present only in specific domains and obviously have arisen late during evolution. In an evolutionary fine-tuning process, these enzymes must have played an essential role in the progressive introduction of new amino acids, and in the refinement and standardization of the canonical nuclear genetic code observed in all extant organisms (functional convergent evolutionary hypothesis).

Keywords: tRNA, Translation, Genetic code, Modified nucleosides, Wobble base-pairing, Evolution, Archaea, Bacteria, Eukarya, Mitochondria

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PII: S0014-5793(09)00965-X

doi:10.1016/j.febslet.2009.11.052

FEBS Letters
Volume 584, Issue 2 , Pages 252-264, 21 January 2010