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Article

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

Molecular and cellular biology - 1 Nov 2004

Liu Shihui, Milne G Todd, Kuremsky Jeffrey G, Fink Gerald R, Leppla Stephen H

Abstract excerpt

Diphthamide, a posttranslational modification of translation elongation factor 2 that is conserved in all eukaryotes and archaebacteria and is the target of diphtheria toxin, is formed in yeast by the actions of five proteins, Dph1 to -5, and a still unidentified amidating enzyme. Dph2 and Dph5 were previously identified. Here, we report the identification of the remaining three yeast proteins (Dph1, -3, and -4)...

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Identifiers

PMID: 15485916
DOI: 10.1128/MCB.24.21.9487-9497.2004
PMCID: PMC522255

Genes

DPH2

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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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.PMID 15485916Read ↗

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Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development.Semantic proximity Read ↗

The biosynthesis and biological function of diphthamideSemantic proximity Read ↗

The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network.Semantic proximity Read ↗

DPH1 and DPH2 variants that confer susceptibility to diphthamide deficiency syndrome in human cells and yeast models.Semantic proximity Read ↗

ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological PerspectivesSemantic proximity Read ↗

DPH1 Gene Mutations Identify a Candidate SAM Pocket in Radical Enzyme Dph1•Dph2 for Diphthamide Synthesis on EF2.Semantic proximity Read ↗

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Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development.Semantic proximity Read ↗

<em>DPH1 </em>Gene Mutations Identify a Candidate SAM Pocket in Radical Enzyme Dph1•Dph2 for Diphthamide Synthesis on EF2Semantic proximity Read ↗

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

Functional Integrity of Radical SAM Enzyme Dph1•Dph2 Requires Non-canonical Cofactor Motifs with Tandem CysteinesSemantic proximity Read ↗

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