| http://purl.uniprot.org/citations/12651896 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12651896 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12651896 | http://www.w3.org/2000/01/rdf-schema#comment | "Initiation factor 3 (eIF3) forms a multifactor complex (MFC) with eIF1, eIF2, and eIF5 that stimulates Met-tRNA(i)(Met) binding to 40S ribosomes and promotes scanning or AUG recognition. We have previously characterized MFC subcomplexes produced in vivo from affinity-tagged eIF3 subunits lacking discrete binding domains for other MFC components. Here we asked whether these subcomplexes can bind to 40S ribosomes in vivo. We found that the N- and C-terminal domains of NIP1/eIF3c, the N- and C-terminal domains of TIF32/eIF3a, and eIF5 have critical functions in 40S binding, with eIF5 and the TIF32-CTD performing redundant functions. The TIF32-CTD interacted in vitro with helices 16-18 of domain I in 18S rRNA, and the TIF32-NTD and NIP1 interacted with 40S protein RPS0A. These results suggest that eIF3 binds to the solvent side of the 40S subunit in a way that provides access to the interface side for the two eIF3 segments (NIP1-NTD and TIF32-CTD) that interact with eIF1, eIF5, and the eIF2/GTP/Met-tRNA(i)(Met) ternary complex."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.org/dc/terms/identifier | "doi:10.1101/gad.1065403"xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.org/dc/terms/identifier | "doi:10.1101/gad.1065403"xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Shin B.-S."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Shin B.-S."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Hinnebusch A.G."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Hinnebusch A.G."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Nielsen K.H."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Nielsen K.H."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Valasek L."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Valasek L."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Mathew A.A."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Mathew A.A."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Szamecz B."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/author | "Szamecz B."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/name | "Genes Dev."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/name | "Genes Dev."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/pages | "786-799"xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/pages | "786-799"xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/title | "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo."xsd:string |
| http://purl.uniprot.org/citations/12651896 | http://purl.uniprot.org/core/title | "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo."xsd:string |