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Phosphorylation of elongation factor 1 in polyribosome fraction of rabbit reticulocytes
Author(s) -
Davydova E.K.,
Sitikov A.S.,
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)81206-5
Subject(s) - polysome , eukaryotic translation elongation factor 1 alpha 1 , phosphorylation , elongation factor , incubation , elongation , protein biosynthesis , biochemistry , chemistry , alpha (finance) , biophysics , biology , ribosome , rna , materials science , medicine , construct validity , nursing , ultimate tensile strength , patient satisfaction , metallurgy , gene
A single protein, M r , ~ 50000, is shown to be phosphorylated during incubation of a mono‐ and polyribosome fraction of rabbit reticulocytes with [γ‐ 32 P]ATP at a low ionic strength. This protein has been identified as the elongation factor 1α (EF‐1α). The phosphorylated EF‐1α, in contrast to the unmodified factor, is not detected in complexes with mono‐ and polyribosomes. It is suggested that the phosphorylation of EF‐lα can result in its decompartmentation from polyribosomes and thus affect the rate of protein synthesis.