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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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]


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