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Diphthamide is a unique posttranslationally modified histidine found only in translation elongation factor-2 (EEF2\; MIM 130610).
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immunotoxin resistance is associated with reversible CpG island methylation and silencing of DPH4 gene transcription
We report here the solution structure and mechanism of novel iron-mediated functional roles of human Dph4, a type III J-protein playing a vital role in diphthamide biosynthesis and normal development.
A mouse that was mutant for the gene, Dph4, was identified.
Diphthamide is a unique posttranslationally modified histidine found only in translation elongation factor-2 (EEF2\; MIM 130610). This modification is conserved from archaebacteria to humans and serves as the target for ADP-ribosylation and inactivation of EEF2 by diphtheria toxin (DT) and Pseudomonas exotoxin A. DPH4 is 1 of several enzymes involved in synthesis of diphthamide in EEF2 (Liu et al., 2004
DnaJ (Hsp40) homolog, subfamily C, member 24
, CSL-type zinc finger-containing protein 3
, DPH4 homolog (JJJ3, S. cerevisiae)
, DPH4, JJJ3 homolog
, dnaJ homolog subfamily C member 24
, zinc finger, CSL domain containing 3
, zinc finger, CSL-type containing 3
, DPH4 homolog
, j domain protein DjC7