Charakterizace dvou nejmensich podjednotek eIF3 a jejich úloh v translaci.

Cuchalová, Lucie

Protein synthesis or mRNA translation is a complex and highly conserved process. Translation consists of initiation, elongation, termination, and ribosome recycling stages. Since most regulation occurs during initiation, its mechanism is being studied intensively to elucidate the molecular basis of every potential control point. The initiation factor eIF3, which in yeast consists of five essential core subunits (eIF3a/TIF32, b/PRT1, c/NIP1, g/TIF35, and i/TIF34) and one transiently associated, non-essential subunit (j/HCR1), is undisputedly one of the key promoters of initiation. In addition, it has also been implicated in playing a critical role during ribosomal recycling, reinitiation, signal transduction, NMD etc. We have focused on determining the molecular mechanism of the roles of eIF3 and its associated eIFs not only in translation initiation but also in termination and in reinitiation. This included the biochemical and genetic mapping of yeast eIF3 binding site on the small ribosomal subunit, among others. We showed that the interaction between the residues 200-400 of a/TIF32-NTD and flexible C-terminal tail RPS0A significantly stimulates attachment of eIF3 and its associated eIFs to small ribosomal subunits in vivo, thus a/TIF32-NTD together with the recently published PCI (proteasome...

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