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The life and death of translation elongation factor 2

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The life and death of translation elongation factor 2. / Jørgensen, Rene; Merrill, A.R.; Andersen, Gregers Rom.

In: Biochem. Soc. Trans., Vol. 34, 2006, p. 1-6.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearch

Harvard

Jørgensen, R, Merrill, AR & Andersen, GR 2006, 'The life and death of translation elongation factor 2', Biochem. Soc. Trans., vol. 34, pp. 1-6.

APA

Jørgensen, R., Merrill, A. R., & Andersen, G. R. (2006). The life and death of translation elongation factor 2. Biochem. Soc. Trans., 34, 1-6.

CBE

Jørgensen R, Merrill AR, Andersen GR. 2006. The life and death of translation elongation factor 2. Biochem. Soc. Trans. 34:1-6.

MLA

Jørgensen, Rene, A.R. Merrill, and Gregers Rom Andersen. "The life and death of translation elongation factor 2". Biochem. Soc. Trans. 2006, 34. 1-6.

Vancouver

Jørgensen R, Merrill AR, Andersen GR. The life and death of translation elongation factor 2. Biochem. Soc. Trans. 2006;34:1-6.

Author

Jørgensen, Rene ; Merrill, A.R. ; Andersen, Gregers Rom. / The life and death of translation elongation factor 2. In: Biochem. Soc. Trans. 2006 ; Vol. 34. pp. 1-6.

Bibtex

@article{d0437fd0b06d11dbbee902004c4f4f50,
title = "The life and death of translation elongation factor 2",
abstract = "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.",
keywords = "toxin, translation, phosphorylation",
author = "Rene J{\o}rgensen and A.R. Merrill and Andersen, {Gregers Rom}",
year = "2006",
language = "English",
volume = "34",
pages = "1--6",
journal = "Biochem. Soc. Trans.",

}

RIS

TY - JOUR

T1 - The life and death of translation elongation factor 2

AU - Jørgensen, Rene

AU - Merrill, A.R.

AU - Andersen, Gregers Rom

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - toxin

KW - translation

KW - phosphorylation

M3 - Review

VL - 34

SP - 1

EP - 6

JO - Biochem. Soc. Trans.

JF - Biochem. Soc. Trans.

ER -