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PMID: 272626 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Phosphorylation of eukaryotic protein synthesis initiation factors.

Benne R, Edman J, Traut RR, Hershey JW

Abstract

Phosphorylation of eukaryotic initiation factors was examined both in intact cells and in vitro with purified components. Intact rabbit reticulocytes were incubated in a medium containing[32P]phosphate, and eight initiation factors were isolated and partially purified. The purified factors were analyzed on dodecyl sulfate/polyacrylamide gels and compared with highly purified nonradioactive factors. Significant amounts of radioactivity were found associated with initiation factors eIF-2, polypeptide 2 (molecular weight 53,000); eIF-3, polypeptides 2 and 4 (molecular weights 110,000 and 67,000); and eIF-4B. Purfied initiation factors from rabbit reticulocytes were also treated in vitro with [gamma-32P]ATP and a cyclic AMP-independent protein kinase isolated from rabbit erythrocytes. Only the factor polypeptides phosphorylated intracellularly were phosphorylated in vitro. The results suggest that the cyclic AMP-independent protein kinase is responsible for the phosphorylation of specific initiation factors in cells active in protein synthesis and that it may play a role in regulating translation.

MeSH Terms
Animals Electrophoresis, Polyacrylamide Gel Molecular Weight Peptide Initiation Factors Phosphoproteins/blood,metabolism Protein Kinases/blood,metabolism Rabbits Reticulocytes/metabolism
Chemicals
Peptide Initiation Factors Phosphoproteins Protein Kinases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Benne R
Edman J
Traut R R
Hershey J W
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1978-01-00
Pages
108-12
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC411193
Subset
IM
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