The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast

In eukaryotes, the m(7)GpppN cap structure is added to all nascent RNA polymerase II transcripts, and serves important functions at multiple steps of RNA metabolism. The predominantly nuclear cap-binding complex (CBC) binds to the cap during RNA synthesis. The predominantly cytoplasmic eukaryotic in...

Descripción completa

Detalles Bibliográficos
Autores: Baron-Benhamou, J. (Julie)|||/items/7db6949d-a485-4cfc-90ab-dfdfe1301d2e, Fortes, P. (Puri)|||/items/4b719a39-983d-402a-bb2a-2bdd276be18e, Inada, T. (Toshifumi)|||/items/1852aa00-6b93-4510-8067-1f185f288b44, Preiss, T. (Thomas)|||/items/015d971e-5fb8-46fb-ad35-3507576e013d, Hentze, M.W. (Matthias W.)|||/items/8ebd4b6c-a7e6-46d8-be24-72673e358fcc
Tipo de recurso: artículo
Fecha de publicación:2003
País:España
Institución:Universidad de Navarra
Repositorio:Dadun. Depósito Académico Digital de la Universidad de Navarra
Idioma:inglés
OAI Identifier:oai:dadun.unav.edu:10171/23328
Acceso en línea:https://hdl.handle.net/10171/23328
Access Level:acceso abierto
Palabra clave:Cap-binding protein
CBC
eIF4E
“pioneer round” of translation
Descripción
Sumario:In eukaryotes, the m(7)GpppN cap structure is added to all nascent RNA polymerase II transcripts, and serves important functions at multiple steps of RNA metabolism. The predominantly nuclear cap-binding complex (CBC) binds to the cap during RNA synthesis. The predominantly cytoplasmic eukaryotic initiation factor 4F (eIF4F) is thought to replace CBC after export of mature mRNA to the cytoplasm, and mediates the bulk of cellular translation. Yeast as well as mammalian CBC interacts in vitro with eIF4G, a subunit of eIF4F. In this work, we investigate a potential role of this interaction during translation in yeast. We identify a mutation (DR548/9AA) in Tif4631p, one of two isoforms of yeast eIF4G, that abolishes its binding to CBC. Cells expressing this mutant protein as the sole source of eIF4G grow at wild-type rates, and bulk cellular translation, as assessed by metabolic labeling and polysome profile analysis, is unchanged. Importantly, we find that the DR548/9AA mutation neither diminishes nor delays the translation of newly induced reporter mRNA. Finally, microarray analysis reveals marked transcriptome alterations in CBC subunit deletion strains, whereas eIF4G point mutants have essentially a wild-type transcriptome composition. Collectively, these data suggest that in yeast, the phenotypic consequences of CBC deletions are separable from its interaction with eIF4G, and that the CBC-eIF4G interaction is dispensable for a potential "pioneering round" of translation in yeast.