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 |
Externí odkaz: |
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