Abstract
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 (i) binding to and elution from m7GDP-agarose columns and (ii) 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.
Original language | English (US) |
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Pages (from-to) | 6085-6089 |
Number of pages | 5 |
Journal | Biochemistry |
Volume | 24 |
Issue number | 22 |
DOIs | |
State | Published - Oct 1 1985 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry