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Endogenous ADP‐ribosylation of elongation factor 2 in polyribosome fraction of rabbit reticulocytes
Author(s) -
Sitikov A.S.,
Davydova E.K.,
Ovchinnikov L.P.
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)80953-9
Subject(s) - polysome , endogeny , elongation factor , incubation , adp ribosylation , biochemistry , nad+ kinase , elongation , polyacrylamide gel electrophoresis , chemistry , in vivo , protein biosynthesis , enzyme , microbiology and biotechnology , biology , rna , ribosome , gene , metallurgy , ultimate tensile strength , materials science
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 [ 32 P]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.
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