Molecular cloning and functional expression of a human cDNA encoding translation initiation factor 6
Open Access
- 23 December 1997
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (26), 14285-14290
- https://doi.org/10.1073/pnas.94.26.14285
Abstract
Eukaryotic translation initiation factor 6 (eIF6) binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. In this paper, we devised a procedure for purifying eIF6 from rabbit reticulocyte lysates and immunochemically characterized the protein by using antibodies isolated from egg yolks of laying hens immunized with rabbit eIF6. By using these monospecific antibodies, a 1.096-kb human cDNA that encodes an eIF6 of 245 amino acids (calculated Mr 26,558) has been cloned and expressed in Escherichia coli. The purified recombinant human protein exhibits biochemical properties that are similar to eIF6 isolated from mammalian cell extracts. Database searches identified amino acid sequences from Saccharomyces cerevisiae, Drosophila, and the nematode Caenorhabditis elegans with significant identity to the deduced amino acid sequence of human eIF6, suggesting the presence of homologues of human eIF6 in these organisms.Keywords
This publication has 26 references indexed in Scilit:
- Function of Eukaryotic Translation Initiation Factor 1A (eIF1A) (Formerly Called eIF-4C) in Initiation of Protein SynthesisJournal of Biological Chemistry, 1997
- Characterization of Multiple mRNAs That Encode Mammalian Translation Initiation Factor 5 (eIF-5)Journal of Biological Chemistry, 1996
- Initiation of Protein Synthesis in Eukaryotic CellsEuropean Journal of Biochemistry, 1996
- Regulation of Translation in Eukaryotic SystemsAnnual Review of Cell and Developmental Biology, 1992
- Effects of eucaryotic initiation factor 3 on eucaryotic ribosomal subunit equilibrium and kineticsBiochemistry, 1988
- Studies on native ribosomal subunits from rat liver. Purification and characterization of a ribosome dissociation factorBiochemistry, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Structural dynamics of bacterial ribosomes: I. Characterization of vacant couples and their relation to complexed ribosomesJournal of Molecular Biology, 1973
- Role of Subunits in the Ribosome CycleNature, 1971