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

FEBS Letters

Ovchinnikov, L.P.¹  Davydova, E.K.¹  Bezlepkina, T.A.¹  Sitikov, A.S.¹  Spirin, A.S.¹ 

[1] Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

关键词: Elongation factor 2;    ADP-ribosylation;    RNA-binding activity;    Protein synthesis regulation;    Compartmentation-decompartmentation;   

DOI  :  10.1016/0014-5793(84)81207-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown