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1 PH4, and DPH5 generated viable cells without diphthamide.
2 cidation of the full biosynthesis pathway of diphthamide.
3 compensates for the loss of the +1 charge on diphthamide.
7 ive studies into the potential regulation of diphthamide, and importantly, its ill-defined biological
8 al modification: the conversion of His699 to diphthamide at the tip of domain IV, the region proposed
11 vel of DPH4 mRNA and protein, which prevents diphthamide biosynthesis and renders EF2 refractory to H
13 ical evidence showing that the first step of diphthamide biosynthesis in the archaeon Pyrococcus hori
18 The evolutionary conservation of the complex diphthamide biosynthesis pathway throughout eukaryotes i
21 verse number of species, including the yeast diphthamide biosynthesis protein-2, dph2, which suggeste
23 hree decades ago, in vitro reconstitution of diphthamide biosynthesis using purified proteins has not
24 ne in yeast is required for the last step of diphthamide biosynthesis, as the deletion of YBR246W lea
26 ty of yeast to zymocin, is also required for diphthamide biosynthesis, implicating DESR1/KTI11 in mul
31 sing agent that, through ADP ribosylation of diphthamide, causes irreversible inactivation of EF2 and
32 ates the eEF2 functional loss resulting from diphthamide deficiency, possibly because the added +1 ch
36 However, recent progress in dissecting the diphthamide gene network (DPH1-DPH7) from the budding ye
43 learly emphasizes a pathobiological role for diphthamide, its physiological function is unclear, and
46 ent protein synthesis in eukaryotes requires diphthamide modification of translation elongation facto
47 normal, whereas dph3-/- mice, which lack the diphthamide modification on eEF-2, are embryonic lethal.
50 tion of proteins, establishes a role for the diphthamide modification, and provides evidence of the a
51 e inactivation still contained predominantly diphthamide-modified eEF2 and were as sensitive to PE an
52 s that cannot make it strongly suggests that diphthamide-modified EF2 occupies an important and trans
53 S(N)1 type mechanism in which attack of the diphthamide nucleophile lags behind departure of the nic
59 eukaryotic translation elongation factor 2, diphthamide represents one of the most intriguing post-t
60 (R)) of eEF2 by bacterial toxins on a unique diphthamide residue inhibits its translocation activity,
61 toxin catalyzes the ADP ribosylation of the diphthamide residue of eukaryotic elongation factor 2 (e
62 duce cholix, a potent protein toxin that has diphthamide-specific ADP-ribosyltransferase activity aga
63 mpact of complete or partial inactivation on diphthamide synthesis and toxin sensitivity, and to addr
65 way and the biochemical players required for diphthamide synthesis but also are likely to foster inno
69 t amidation step, with Dph6 being the actual diphthamide synthetase catalyzing the ATP-dependent amid
70 We found that yeast protein YLR143W is the diphthamide synthetase catalyzing the last amidation ste
71 we identified the previously unknown enzyme diphthamide synthetase for the last step of diphthamide
73 s region is post-translationally modified to diphthamide, the target for Corynebacterium diphtheriae
77 elongation factor-2 at His(715) that yields diphthamide, the target site for ADP ribosylation by DT
81 and to begin to investigate the function of diphthamide, we generated dph3 knockout mice and showed
82 tant elements of the biosynthetic pathway of diphthamide, which are required for the cytotoxic effect
83 lationally modified histidine residue called diphthamide, which is the target of diphtheria toxin.
84 ationally modified histidine residue, termed diphthamide, which serves as the only target for diphthe
85 in the mutant cells revealed a novel form of diphthamide with an additional methyl group that prevent
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