eEF2 (eukaryotic elongation factor 2) occupies an essential role in protein synthesis where it catalyses the translocation of the two tRNAs and the mRNA after peptidyl transfer on the 80 S ribosome. Recent crystal structures of eEF2 and the cryo-electron microscopy reconstruction of its 80 S 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.
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February 2006
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Conference Article|
January 20 2006
The life and death of translation elongation factor 2
R. Jørgensen;
R. Jørgensen
* Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada N1G 2W1
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A.R. Merrill;
A.R. Merrill
* Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada N1G 2W1
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G.R. Andersen
G.R. Andersen
1
† Centre for Structural Biology, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000, Denmark
1 To whom correspondence should be addressed (email gra@mb.au.dk).
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Publisher: Portland Press Ltd
Received:
June 20 2005
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2006 The Biochemical Society
2006
Biochem Soc Trans (2006) 34 (1): 1–6.
Article history
Received:
June 20 2005
Citation
R. Jørgensen, A.R. Merrill, G.R. Andersen; The life and death of translation elongation factor 2. Biochem Soc Trans 1 February 2006; 34 (1): 1–6. doi: https://doi.org/10.1042/BST0340001
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