Home > Conference materials > Papers > The C-terminal domain of eIF3c/NIP1 and eIF3j/HCR1 subunits of yeast eIF3 seem to promote its association with the 40S ribosome by making contacts with the small subunit proteins RPS33/ASC1 and RPS2, respectively
Original title:
The C-terminal domain of eIF3c/NIP1 and eIF3j/HCR1 subunits of yeast eIF3 seem to promote its association with the 40S ribosome by making contacts with the small subunit proteins RPS33/ASC1 and RPS2, respectively
Translated title:
C-konc. segment NIP1/eIF3c a HCR1 subjednotky eIF3 umožňují jeho vazbu na 40S ribozóm přes RPS33/ASC1 a RPS22
Authors:
Rutkai, Edit ; Herrmannová, Anna ; Szamecz, Bela ; 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] One of the rst critical steps of protein synthesis is the recruitment of the eIF2.GTP.Met-tRNAiMet ternary complex (TC) to the 40S ribosome. In yeast, the TC occurs together with eIFs 1, 3 and 5 in a Multifactor complex (MFC) that was shown to function as an important intermediate of the initiation pathway. Our previous study determined several critical domains of the TIF32 and NIP1 subunits of yeast eIF3, the deletion of which, in the background of a wild type gene, signifcantly aected binding of the mutant MFC to the 40S ribosomes. Subsequent identifcation of the two contact points between TIF32 and components of the 40S ribosome enabled us to propose that the major body of the eIF3 complex resides under the head region on the solvent side of the small ribosomal subunit facing down towards its left footPráce pojednáva o studiu inciace translace a specifické úloze translačního iniciačního faktoru eIF3
Keywords:
eif3; translation Project no.: CEZ:AV0Z50200510 (CEP), The Wellcome Trust grant to LV, FIC NIH GRIP grant to LV Funding provider: GB, XE Host item entry: Translational Control and Non-Coding RNA
Institution: Institute of Microbiology AS ČR
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Document availability information: Fulltext is available at the institute of the Academy of Sciences. Original record: http://hdl.handle.net/11104/0145410