1-N6-Etheno-ADP-ribosylation of elongation factor-2 by diphtheria toxin.

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 Lett

journal_title

FEBS letters

authors

Giovane A,Balestrieri C,Quagliuolo L,Servillo L

doi

10.1016/0014-5793(85)80006-5

subject

Has Abstract

pub_date

1985-10-28 00:00:00

pages

191-4

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(85)80006-5

journal_volume

191

pub_type

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