Purification and characterization of protein synthesis initiation factor eIF-4E from the yeast Saccharomyces cerevisiae.
A 24 000-dalton protein [yeast eukaryotic initiation factor 4E (eIF-4E)] was purified from yeast Saccharomyces cerevisiae postribosomal supernatant by m7GDP-agarose affinity chromatography. The protein behaves very similarly to mammalian protein synthesis initiation factor eIF-4E with respect to binding to and elution from m7GDP-agarose columns and cross-linking to oxidized reovirus mRNA cap structures. Yeast eIF-4E is required for translation as shown by the strong and specific inhibition of cell-free translation in a yeast extract by a monoclonal antibody directed against yeast eIF-4E.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D002474:Cell-Free System; D002846:Chromatography, Affinity; D039561:Eukaryotic Initiation Factor-4E; D007700:Kinetics; D008970:Molecular Weight; D010448:Peptide Initiation Factors / Q000302:isolation & purification* / Q000378:metabolism; D014176:Protein Biosynthesis; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*
D000906:Antibodies; D000936:Antigen-Antibody Complex; D039561:Eukaryotic Initiation Factor-4E; D010448:Peptide Initiation Factors