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- W58357415 abstract "The elongation factor 2 (EF-2) catalyzes translocation, which is the last step of the elongation cycle in the course of protein synthesis. The factor is the only known protein that is ADP-ribosylated by diphtheria toxin in the presence of NAD. The target of this reaction is a post-translationally modified histidine residue, called diphthamide. ADP-ribosylated EF-2 is unable to translocate, but still retains the ability to form a ternary complex with GDP and ribosome (1). We demonstrated that diphtheria toxin is able to recognize as a substrate an NAD analog, nicotinamide 1,N6 ethenoadeninedinucleotide (ε NAD), and to transfer the fluorescent ε ADP-ribose moiety onto the EF-2 diphthamide residue (2). Therefore, it was possible to label the EF-2 with this fluorescent probe by an efficient and selective enzymatic mechanism which allowed us to confidently attribute the molecular localization of the fluorophore at the level of the diphthamide residue." @default.
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- W58357415 date "1987-01-01" @default.
- W58357415 modified "2023-09-26" @default.
- W58357415 title "Studies on the Interaction between Ribosome and Elongation Factor 2 by Fluorescent Labeling of the Diphtamide Residue" @default.
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- W58357415 doi "https://doi.org/10.1007/978-1-4612-4600-8_17" @default.
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