The role of mammalian initiation factor eIF-4D and its hypusine modification in translation

John W.B. Hershey, Zeljka McBride, Joachim Schnier

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27 Scopus citations


Initiation factor eIF-4D functions late in the initiation pathway, apparently during formation of the first peptide bond. The factor is post-translationally modified at a specific lysine residue by reaction with spermidine and subsequent hydroxylation to form hypusine. A precursor form lacking hypusine is inactive in the assay for methionyl-puromycin synthesis, but activity is restored following in vitro modification to deoxyhypusine, thereby suggesting that the modification is essential for function. Since formylated methionyl-tRNA is less dependent on eIF-4D in the puromycin assay, we postulate that eIF-4D and its hypusine modification may stabilize charged Met-tRNA binding to the peptidyl transferase center of the 60S ribosomal subunit. Analysis of eIF-4D genes in yeast indicate that eIF-4D and its hypusine modification are essential for cell growth.

Original languageEnglish (US)
Pages (from-to)160-162
Number of pages3
JournalBBA - Gene Structure and Expression
Issue number1-3
StatePublished - Aug 27 1990



  • Hypusine
  • Initiation factor
  • Protein synthesis
  • Puromycin
  • Yeast

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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