Eukaryotic elongation factor 2 loses its non-specific affinity for RNA and leaves polyribosomes as a result of ADP-ribosylation.

Autor: Sitikov AS, Davydova EK, Bezlepkina TA, Ovchinnikov LP, Spirin AS
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 1984 Oct 29; Vol. 176 (2), pp. 406-10.
DOI: 10.1016/0014-5793(84)81207-7
Abstrakt: ADP-ribosylation of rabbit reticulocyte elongation factor 2 (EF-2) catalyzed by the A fragment of diphtheria toxin leads to a loss of its non-specific affinity for RNA. The removal of the ADP-ribose residue from EF-2 in the reverse reaction with nicotinamide restores its affinity for RNA. ADP-ribosylation of EF-2 is accompanied by its dissociation from the complexes with mono- and polyribosomes detected in the rabbit reticulocyte lysate at low ionic strength. The loss of the non-specific affinity of EF-2 for RNA as a result of ADP-ribosylation and, as a consequence, its decompartmentation from polyribosomes is assumed to be a reason for the diphtheria toxin-induced inactivation of the factor in eukaryotic cells.
Databáze: MEDLINE