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- W109668503 abstract "eIF-4F, a multi-protein mRNA cap binding complex, was purified from HeLa cell S10 by m/sup 7/G-Sepharose-4B chromatography. The m/sup 7/GTP eluate was analyzed by 2-dimensional gel electrophoresis. The most abundant protein is eIF-4E (CBP-I), which exhibits two isoelectric forms. The more acidic (30%) labels with (/sup 32/P)phosphate in vivo and is lost when samples are treated with phosphatase. Analysis of heat shocked lysates reveals that eIF-4E becomes dephosphorylated, possibly accounting for the reported loss of eIF-4E activity in stressed cells. The m/sup 7/GTP eluates from normal cells also contain the other eIF-4F subunits, eIF-4A and p220, but in lower molar amounts, suggesting only part of the eIF-4E forms eIF-4F complexes. In addition, virtually all of the subunits of eIF-3 are present in amounts exceeding that of eIF-4A. eIF-4B also binds to the affinity column and elutes either with the GDP or m/sup 7/GTP washes, depending on extraction and binding conditions. The results suggest that all four initiation factors (eIF-3, eIF-4A, eIF-4B and eIF-4F) form a supermolecular complex which may be the active form of the factors for mRNA binding. Analyses of heat shocked lysates show reduced recoveries of eIF-3, eIF-4A and p220. The stability and activity of the complex correlatesmore » with the phosphorylation of the eIF-4E subunit, and thus phosphorylation may regulate the activity of eIF-4F in HeLa cells.« less" @default.
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- W109668503 date "1986-05-01" @default.
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- W109668503 title "Initiation factor eIF-4F: phosphorylation and interaction with other initiation factors" @default.
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