Purification and characterization of protein synthesis initiation factor eIF-4E from the yeast Saccharomyces cerevisiae
Altmann, M.; Edery, I.; Sonenberg, N.; Trachsel, H.
Biochemistry 24(22): 6085-6089
1985
ISSN/ISBN: 0006-2960
PMID: 3910088
DOI: 10.1021/bi00343a009
Accession: 041135402
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.