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The life and death of translation elongation factor 2

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  • Faculty of Science
  • Department of Molecular Biology
The eukaryotic elongation factor 2 (eEF2) occupies an essential role in protein synthesis where it catalyses the translocation of the two tRNAs and the mRNA after peptidyl transfer on the 80S ribosome. Recent crystal structures of eEF2 and the cryo-EM reconstruction of its 80S complex now provide a substantial structural framework for dissecting the functional properties of this factor. The factor can be modified by either phosphorylation or ADP-ribosylation which results in cessation of translation. We review the structural and functional properties of eEF2 with particular emphasis on the unique diphthamide residue, which is ADP-ribosylated by diphtheria toxin from Corynebacterium diphtheriae and exotoxin A from Pseudomonas aeruginosa.
Original languageEnglish
JournalBiochem. Soc. Trans.
Volume34
Pages (from-to)1-6
Number of pages6
Publication statusPublished - 2006

    Research areas

  • toxin, translation, phosphorylation

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