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Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation.

The yeast translation factor eIF4G associates with both the cap-binding protein eIF4E and the poly(A)-binding protein Pab1p. Here we report that the two yeast eIF4G homologs, Tif4631p and Tif4632p, share a conserved Pab1p-binding site. This site is required for Pab1p and poly(A) tails to stimulate the in vitro translation of uncapped polyadenylylated mRNA, and the region encompassing it is required for the cap and the poly(A) tail to synergistically stimulate translation. This region on Tif4631p becomes essential for cell growth when the eIF4E binding site on Tif4631p is mutated. Pab1p mutations also show synthetic lethal interactions with eIF4E mutations. These data suggest that eIF4G mediates poly(A) tail stimulated translation in vitro, and that Pab1p and the domain encompassing the Pab1p-binding site on eIF4G can compensate for partial loss of eIF4E function in vivo.

Pubmed ID: 9256432

Authors

  • Tarun SZ
  • Wells SE
  • Deardorff JA
  • Sachs AB

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Data

August 19, 1997

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Binding Sites
  • Eukaryotic Initiation Factor-4F
  • Eukaryotic Initiation Factor-4G
  • Fungal Proteins
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Initiation Factors
  • Protein Biosynthesis
  • RNA, Messenger
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins