eif5A promotes translation of polyproline motifs

Erik Gutierrez, Byung Sik Shin, Christopher J. Woolstenhulme, Joo Ran Kim, Preeti Saini, Allen R. Buskirk, Thomas E. Dever

Research output: Contribution to journalArticlepeer-review

244 Scopus citations


Translation factor eIF5A, containing the unique amino acid hypusine, was originally shown to stimulate Met-puromycin synthesis, a model assay for peptide bond formation. More recently, eIF5A was shown to promote translation elongation; however, its precise requirement in protein synthesis remains elusive. We use invivo assays in yeast and invitro reconstituted translation assays to reveal a specific requirement for eIF5A to promote peptide bond formation between consecutive Pro residues. Addition of eIF5A relieves ribosomal stalling during translation of three consecutive Pro residues invitro, and loss of eIF5A function impairs translation of polyproline-containing proteins invivo. Hydroxyl radical probing experiments localized eIF5A near the E site of the ribosome with its hypusine residue adjacent to the acceptor stem of the P site tRNA. Thus, eIF5A, like its bacterial ortholog EFP, is proposed to stimulate the peptidyl transferase activity of the ribosome and facilitate the reactivity of poor substrates like Pro.

Original languageEnglish (US)
Pages (from-to)35-45
Number of pages11
JournalMolecular cell
Issue number1
StatePublished - Jul 11 2013
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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