Original title: Partial deletion of the RPS0A-binding domain of TIF32/eIF3A affects 40S ribosome-association of the multifactor complex and severely impairs reinitiation on the GCN4 mRNA leader
Translated title: Delece RPS0A-vazebné domény TIF32/eIF3A brání vazbě MFC na 40S ribozóm a blokuje derepresi GCN4 exprese
Authors: Szamecz, Bela ; Rutkai, Edit ; Nielsen, K. H. ; Valášek, Leoš
Document type: Papers
Conference/Event: Translational Control and Non-Coding RNA Meeting, Nové Hrady (CZ), 2006-12-08 / 2006-12-12
Year: 2006
Language: eng
Abstract: [eng] [cze]
Yeast Initiation factor 3 (eIF3) occurs together with the eIF2.GTP.Met-tRNAiMet ternary complex (TC) and eIFs 1 and 5 in a pre-formed unit designated the multifactor complex (MFC) that was implicated in playing a critical role in ecient recruitment of TC and mRNA to the 40S ribosomes and stimulation of the post-assembly processes such as scanning and AUG recognition. In ecort to identify binding sites of the MFC on the 40S ribosome, we previously demonstrated that deletion of the rst 199 amino acids of the N-terminal domain (NTD) of the TIF32 subunit of eIF3/eIF3a, in the presence of a wild-type gene, completely eliminated association of the mutant MFC with the 40S ribosome without aecting its overall integrity. In addition, we showed that the TIF32-NTD contains a binding site for the C-terminal domain (CTD) of the small ribosomal protein 0A (RPS0A) that is located on the solvent side of the 40S subunit where the main body of eIF3 was proposed to reside Práce pojednáva o studiu inciace translace a specifické úloze translačního iniciačního faktoru eIF3
Keywords: gcn4; translation
Project no.: CEZ:AV0Z50200510 (CEP), The Wellcome Trust grant to LV
Funding provider: XE
Host item entry: Translational Control and Non-Coding RNA

Institution: Institute of Microbiology AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0145412

Permalink: http://www.nusl.cz/ntk/nusl-37006


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