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PMID: 272635 Published · ppublish English Journal Article

Binding and release of eukaryotic initiation factor eIF-2 and GTP during protein synthesis initiation.

Trachsel H, Staehelin T

Abstract

The eukaryotic initiation factor eIF-2 forms a ternary complex with Met-tRNAf and GTP. This complex binds to the 40S ribosomal subunit in the absence of mRNA and mRNA binding factors. Highly purified eIF-2 from rabbit reticulocytes was labeled with 125I by using the Bolton-Hunter reagent or with [gamma-32P]ATP by using the heme-regulated translational inhibitor protein kinase. The labeled eIF-2 was bound, together with equimolar amounts of Met-tRNAf and GTP, to the 40S subunit. In the presence of mRNA, mRNA binding factors, and 60S ribosomal subunits (complete initiation assay), eIF-2 was released from the 40S initiation complex in the subunit joining reaction. GTP also was released in this step and probably was hydrolyzed in the reaction that is dependent upon eIF-5 and the 60S subunit. The function of phosphorylated eIF-2 in initiation of protein synthesis is discussed.

MeSH Terms
Animals Guanosine Triphosphate/metabolism Peptide Chain Initiation, Translational Peptide Initiation Factors Phosphates/metabolism Protein Binding RNA, Transfer/metabolism Rabbits Ribosomes/metabolism
Chemicals
Peptide Initiation Factors Phosphates Guanosine Triphosphate RNA, Transfer
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Trachsel H
Staehelin T
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21 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
204-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC411214
Subset
IM
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