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PROSITE documentation PDOC51074 [for PROSITE entry PS51074]

Zinc finger DPH-type profile


Diphthamide is a unique post-translationally modified histidine residue found only in translation elongation factor 2 (eEF-2). It is conserved from archaebacteria to humans and serves as the target for diphteria toxin and Pseudomonas exotoxin A. These two toxins catalyze the transfer of ADP-ribose to diphtamide on eEF-2, thus inactivating eEF-2, halting cellular protein synthesis, and causing cell death [1].

The biosynthesis of diphtamide is dependent on at least five proteins, DPH1 to -5, and a still unidentified amidating enzyme. DPH3 and DPH4 share a conserved region which encode a putative zinc finger, the DHP-type or CSL-type (after the conserved motif of the final cysteine) zinc finger [2,3]. The function of this motif is unknown.

The profile we developed covers the whole DPH-type zinc finger.

Last update:

January 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ZF_DPH, PS51074; Zinc finger DPH-type profile  (MATRIX)


1AuthorsCollier R.J.
TitleUnderstanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century.
SourceToxicon 39:1793-1803(2001).
PubMed ID11595641

2AuthorsLiu S. Leppla S.H.
TitleRetroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins.
SourceMol. Cell 12:603-613(2003).
PubMed ID14527407

3AuthorsLiu S. Milne G.T. Kuremsky J.G. Fink G.R. Leppla S.H.
TitleIdentification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.
SourceMol. Cell. Biol. 24:9487-9497(2004).
PubMed ID15485916

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