Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes

Endogenous ADP-ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes

Several polypeptides of about 120, 96, 85, 60 and 38 kDa are shown to be radiolabeled during incubation of the mono- and polyribosome fraction of rabbit reticulocytes with [ 32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacr...

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Veröffentlicht in:FEBS letters 1984-10, Vol.176 (1), p.261-263
Hauptverfasser: Sitikov, A.S., Davydova, E.K., Ovchinnikov, L.P.
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Diphosphate Ribose - metabolism
ADP-ribosylation
Animals
Biological and medical sciences
Elongation factor 2
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
Molecular genetics
NAD - metabolism
Nucleoside Diphosphate Sugars - metabolism
Nucleotidyltransferases - metabolism
Peptide Elongation Factor 2
Peptide Elongation Factors - metabolism
Poly(ADP-ribose) Polymerases
Polyribosome
Polyribosomes - metabolism
Protein biosynthesis regulation
Rabbit reticulocyte
Rabbits
Reticulocytes - metabolism
Translation. Translation factors. Protein processing
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Zusammenfassung:Several polypeptides of about 120, 96, 85, 60 and 38 kDa are shown to be radiolabeled during incubation of the mono- and polyribosome fraction of rabbit reticulocytes with [ 32P]NAD. Among them is a polypeptide coinciding with elongation factor 2 (EF-2) in its electrophoretic mobility in SDS-polyacrylamide gel. The addition of pure EF-2 to the polyribosome fraction results in an increase of the radioactive label in this polypeptide band. From this it is concluded that both endogenous and added EF-2 is ADP-ribosylated by an enzyme associated with polyribosomes. A possibility of regulation of protein synthesis through endogenous ADP-ribosylation in vivo is considered.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(84)80953-9