Purification and Characterization of Protein Synthesis Initiation Factor eIF-4E from the Yeast Saccharomyces cerevisiae

Michael Altmann, Hans Trachsel, Isaac Edery, Nahum Sonenberg

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

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 languageEnglish (US)
Pages (from-to)6085-6089
Number of pages5
JournalBiochemistry
Volume24
Issue number22
DOIs
StatePublished - Oct 1 1985
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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