Abstract:
:Diphtheria toxin fragment A is able to inhibit protein synthesis in the eukaryotic cell by ADP-ribosylating the diphthamide residue of elongation factor-2 (EF-2) [(1980) J. Biol. Chem. 255, 10710-10720]. The reaction requires NAD as ADP-ribose donor. This work reports on the capacity of an NAD analog, the nicotinamide 1-N6-ethenoadenine dinucleotide (epsilon NAD), to be a substrate of diphtheria toxin fragment A in the transferring reaction of the fluorescent moiety, the epsilon ADP-ribose, to the EF-2. As a consequence of the transfer of the epsilon ADP-ribosyl moiety to the EF-2, there is an increase in the emission intensity of the fluorophore and a blue shift in its emission maximum. The epsilon ADP-ribosylated EF-2, like ADP-ribosylated EF-2, retains the capacity to bind GTP and ribosome. The utility of introducing a fluorescent probe in a well defined point of the EF-2 molecule for conformational or binding studies is discussed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Giovane A,Balestrieri C,Quagliuolo L,Servillo Ldoi
10.1016/0014-5793(85)80006-5subject
Has Abstractpub_date
1985-10-28 00:00:00pages
191-4issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(85)80006-5journal_volume
191pub_type
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