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Article

A mutation in codon 717 of the CHO-K1 elongation factor 2 gene prevents the first step in the biosynthesis of diphthamide.

Somatic cell and molecular genetics - 1 May 1992

Foley B T, Moehring J M, Moehring T J

Abstract excerpt

The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide. The diphthamide residue of EF-2 is the target site for ADP ribosylation by diphtheria toxin and Pseudomonas exotoxin A. ADP-ribosylated EF-2 does not function in protein...

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PMID: 1353910
DOI: 10.1007/BF01233859

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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A mutation in codon 717 of the CHO-K1 elongation factor 2 gene prevents the first step in the biosynthesis of diphthamide.PMID 1353910Read ↗

The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A.Semantic proximity Read ↗

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Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.Semantic proximity Read ↗

The biosynthesis and biological function of diphthamideSemantic proximity Read ↗

A dominant-negative approach that prevents diphthamide formation confers resistance to Pseudomonas exotoxin A and diphtheria toxin.Semantic proximity Read ↗

Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance.Semantic proximity Read ↗

Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development.Semantic proximity Read ↗

Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins.Semantic proximity Read ↗

Modification of the reactivity of three amino-acid residues in elongation factor 2 during its binding to ribosomes and translocation.Semantic proximity Read ↗

Insights into diphthamide, key diphtheria toxin effector.Semantic proximity Read ↗

Characterization of the endogenous ADP-ribosylation of wild-type and mutant elongation factor 2 in eukaryotic cells.Semantic proximity Read ↗

Requirement for prolonged action in the cytosol for optimal protein synthesis inhibition by diphtheria toxin.Semantic proximity Read ↗

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