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1‐ N 6 ‐Etheno‐ADP‐ribosylation of elongation factor‐2 by diphtheria toxin
Author(s) -
Giovane A.,
Balestrieri C.,
Quagliuolo L.,
Servillo L.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80006-5
Subject(s) - nad+ kinase , nicotinamide adenine dinucleotide , adp ribosylation , diphtheria toxin , chemistry , elongation factor , stereochemistry , moiety , gtp' , conformational change , fluorophore , biochemistry , fluorescence , toxin , ribosome , enzyme , rna , physics , quantum mechanics , gene
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‐ N 6 ‐ethenoadenine dinucleotide (ϵNAD), to be a substrate of diphtheria toxin fragment A in the transferring reaction of the fluorescent moiety, the ϵADP‐ribose, to the EF‐2. As a consequence of the transfer of the ϵADP‐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 ϵADP‐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.