Nature 465, 891–896 (2010)
In this Article, the following studies, which led to the identification of diphthamide structure and its biosynthetic genes, should have been cited1,2,3,4,5. Reference 1 reports the presence of an unusual amino acid at the ADP-ribosylation site of elongation factor 2 (EF2); ref. 2 reports the properties of the modified residue in EF2 and proposed the name diphthamide; ref. 3 reports the structure of diphthamide; ref. 4 describes work to suggest that the 3-amino-3-carboxypropyl group of diphthamide come from S-adenosyl methionine; and ref. 5 reports the identification of yeast mutants that are defective in diphthamide biosynthesis and proposes the biosynthetic pathway.
References
Robinson, E. A., Henriksen, O. & Maxwell, E. S. Elongation factor 2. Amino acid sequence at the site of adenosine diphosphate ribosylation. J. Biol. Chem. 249, 5088–5093 (1974)
Van Ness, B. G., Howard, J. B. & Bodley, J. W. ADP-ribosylation of elongation factor by diphtheria toxin: isolation and properties of the novel ribosyl-amino acid and its hydrolysis products. J. Biol. Chem. 255, 10717–10720 (1980)
Van Ness, B. G., Howard, J. B. & Bodley, J. W. ADP-ribosylation of elongation factor 2 by diphtheria toxin: NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products. J. Biol. Chem. 255, 10710–10716 (1980)
Dunlop, P. C. & Bodley, J. W. Biosynthetic labelling of diphthamide in Saccharomyces cerevisiae . J. Biol. Chem. 258, 4754–4758 (1983)
Chen, J. Y., Bodley, J. W. & Livingston, D. M. Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae . Mol. Cell. Biol. 5, 3357–3360 (1985)
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The online version of the original article can be found at 10.1038/nature09138
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Zhang, Y., Zhu, X., Torelli, A. et al. Erratum: Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme. Nature 473, 544 (2011). https://doi.org/10.1038/nature10087
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DOI: https://doi.org/10.1038/nature10087
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