PMID: 3756171Oct 16, 1986Paper

Eukaryotic initiation factor 2 from rat liver: no apparent function for the beta-subunit in the formation of initiation complexes

Biochimica Et Biophysica Acta
D R Colthurst, C G Proud

Abstract

Eukaryotic protein synthesis initiation factor 2 (eIF-2) from rat liver has been resolved into two subfractions by anion-exchange chromatography on DEAE-cellulose. One of these contained all three components (eIF-2 alpha, eIF-2 beta, eIF-2 gamma) characteristic of mammalian eIF-2, whilst the other fraction contained only two. By a number of criteria these were shown to be eIF-2 alpha and eIF-2 gamma. The absence of eIF-2 beta from this fraction was not due to its proteolytic degradation during purification since it was unaffected by the inclusion of a range of proteinase inhibitors in the isolation media. The properties of eIF-2 containing or lacking eIF-2 beta have been directly compared. It was found that eIF-2 beta was not required for the binding of guanine nucleotides to eIF-2 or for formation of ternary initiation complexes with GTP and the initiator tRNA. eIF-2 lacking eIF-2 beta was able to form 40 S initiation complexes and the presence of eIF-2 beta was also unnecessary for the stimulation of eIF-2 activity by the recycling factor, eIF-2B. Some of these findings are at variance with previous reports in which eIF-2 beta was removed proteolytically. The role of eIF-2 beta in the overall physiological function of eIF-2 r...Continue Reading

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Citations

May 17, 2011·Biochemistry. Biokhimii︠a︡·E A Stolboushkina, M B Garber
Oct 18, 1994·Biochimica Et Biophysica Acta·A FlynnA Kaminski
Jul 18, 1993·Biochimica Et Biophysica Acta·A FlynnC G Proud
Mar 6, 1989·Biochimica Et Biophysica Acta·S J ClarkC G Proud
Aug 14, 1987·Biochemical and Biophysical Research Communications·V Felipo, S Grisolía

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