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Eukaryotic elongation factor 2 loses its non‐specific affinity for RNA and leaves polyribosomes as a result of ADP‐ribosylation
Author(s) -
Sitikov A.S.,
Davydova E.K.,
Bezlepkina T.A.,
Ovchinnikov L.P.,
Spirin A.S.
Publication year - 1984
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(84)81207-7
Subject(s) - reticulocyte , adp ribosylation , polysome , rna , diphtheria toxin , biochemistry , elongation factor , chemistry , biology , microbiology and biotechnology , ribosome , toxin , nad+ kinase , enzyme , gene
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.