Isolation and initial characterization of eIF6 – Eukaryotic initiation factor 6 (eIF6), a monomeric protein of about 26.5 kDa, was originally isolated from the postribosomal supernatant of both wheat germ (Russel and Spremulli 1979) and mammalian cell extracts (Valenzuela et al. 1982) based on an in vitro assay that measured the ability of the protein to bind specifically to the 60S ribosomal subunit and to prevent the association of the 60S subunit to the 40S ribosomal subunit to form the 80S ribosomes. Because, the assembly of the 80S initiation complex during initiation of protein synthesis requires a cellular pool of free 40S and 60S ribosomal subunits, eIF6 was thought to play a direct role in the provision of free ribosomal subunits required for initiation of protein synthesis. The protein was therefore classified as a eukaryotic translation initiation factor (eIF), although its function in translation was...
- Basu U, Si K, Deng H, Maitra U. Phosphorylation of mammalian translation initiation factor 6 and its Saccharomyces cerevisiae homologue Tif6p: evidence that phosphorylation of Tif6p regulates its nucleocytoplasmic distribution and is required for yeast cell growth. Mol Cell Biol. 2003;23:6187–99.PubMedPubMedCentralCrossRefGoogle Scholar
- Russel DW, Spremulli LL. Purification and characterization of a ribosome dissociation factor (eukaryotic initiation factor 6) from wheat germ. J Biol Chem. 1979;254:8796–800.Google Scholar