Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos.
The eukaryotic polypeptide chain initiation factor 4F (eIF-4F), purified by m7GTP-Sepharose chromatography from whole extracts of Drosophila melanogaster embryos, consists of two subunits, the previously identified eIF-4E (35 kDa) (Maroto, F. G., and Sierra, J. M. (1989) Mol. Cell. Biol. 9, 2181-2190) and another of 200 kDa. Both subunits cosedimented through a sucrose density gradient containing 0.5 M KCl. In contrast to rabbit reticulocyte eIF-4F, we did not find any RNA-dependent ATPase associated with the Drosophila factor. As shown previously for eIF-4E, the p200 subunit was also required for the translation of endogenous mRNAs in cell-free systems from Drosophila embryos. Only the eIF-4E subunit was able to cross-link to the m7G cap structure. However, an efficient cross-linking of the p200 subunit to an uncapped mRNA was observed. Both subunits were phosphorylated in vitro by protein kinase C from rat brain. As an extension of our previous results (Zapata, J. M., Maroto, F. G., and Sierra, J. M. (1991) J. Biol. Chem. 266, 16007-16014) we found that the translation of the heat shock mRNAs was independent of both of the eIF-4F subunits.[1]References
- Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos. Zapata, J.M., Martínez, M.A., Sierra, J.M. J. Biol. Chem. (1994) [Pubmed]
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