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 t...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1997-08, Vol.94 (17), p.9046-9051
Main Authors: Tarun, S.Z. Jr, Wells, S.E, Deardorff, J.A, Sachs, A.B
Format: Article
Language:English
Subjects:
Amino Acid Sequence
AMINO ACID SEQUENCES
ARN MENSAJERO
ARN MESSAGER
BINDING PROTEINS
BINDING SITES
Binding Sites - genetics
Biochemistry
Biological Sciences
CHEMICAL COMPOSITION
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Eukaryotic Initiation Factor-4F
Eukaryotic Initiation Factor-4G
Fungal Proteins - genetics
Fungal Proteins - metabolism
Genetic mutation
INDUCED MUTATION
MESSENGER RNA
Molecular biology
Molecular Sequence Data
MUTACION INDUCIDA
Mutagenesis
Mutagenesis, Site-Directed
MUTANT
MUTANTES
MUTANTS
MUTATION PROVOQUEE
Peptide initiation factors
Peptide Initiation Factors - genetics
Peptide Initiation Factors - metabolism
Plasmids
POLY(A)-BINDING PROTEIN
POLYADENYLASTED MESSENGER RNA
Protein Biosynthesis
PROTEINAS AGLUTINANTES
PROTEINE DE LIAISON
Proteins
Resins
RNA, Messenger - genetics
RNA, Messenger - metabolism
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae Proteins
Viability
Yeast
Yeasts
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Summary: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
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.17.9046