Abstract
We have isolated [de Haro, C. & Ochoa, S. (1978) Proc. Natl. Acad. Sci. USA 75, 2713-2716] a protein factor (eIF-2 stimulating protein, ESP) that is essential for formation of ternary and 40S initiation complexes by the eukaryotic polypeptide chain initiation factor 2 (eIF-2) at the low concentrations of eIF-2 present in reticulocyte lysates. The fact that stimulation of complex formation by ESP is virtually abolished when the small (38,000 daltons) subunit of eIF-2 is phosphorylated by ATP in the presence of eIF-2 kinase (heme-controlled inhibitor, HCI) is consistent with the notion that HCI inhibits translation in lysates by blocking the interaction of eIF-2 with ESP. Our present work, with highly purified eIF-2 and ESP, has additionally established that, unlike phosphorylation of the small subunit, phosphorylation of the middle (52,000 daltons) subunit of eIF-2, which does not lead to translational inhibition in lysates, does not affect eIF-2-ESP interaction. This provides further support for our model of translational inhibition by HCI.
MeSH Terms
Animals
Bacterial Proteins/isolation & purification,physiology
Escherichia coli/metabolism
Heme/physiology
Kinetics
Molecular Weight
Peptide Chain Initiation, Translational
Peptide Initiation Factors/isolation & purification,metabolism
Protein Biosynthesis
RNA, Transfer/metabolism
Rabbits
Reticulocytes/metabolism
Ribosomes/metabolism
Chemicals
Bacterial Proteins
Peptide Initiation Factors
Heme
RNA, Transfer
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
de Haro C
Ochoa S
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21 references, click to expand
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