Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly

0379099 - MBÚ 2013 RIV GB eng J - Článek v odborném periodiku
Herrmannová, Anna - Daujotyte, D. - Yang, J. - Ch. - Cuchalová, Lucie - Gorrec, F. - Wagner, Susan - Dányi, István - Lukavsky, P. J. - Valášek, Leoš Shivaya
Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly.
Nucleic Acids Research. Roč. 40, č. 5 (2012), s. 2294-2311. ISSN 0305-1048. E-ISSN 1362-4962
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: START CODON SELECTION * RNA RECOGNITION MOTIF * GCN4 MESSENGER-RNA
Kód oboru RIV: CE - Biochemie
Impakt faktor: 8.278, rok: 2012

Translation initiation factor eIF3 acts as the key orchestrator of the canonical initiation pathway in eukaryotes, yet its structure is greatly unexplored. We report the 2.2 A resolution crystal structure of the complex between the yeast seven-bladed beta-propeller eIF3i/TIF34 and a C-terminal alpha-helix of eIF3b/PRT1, which reveals universally conserved interactions. Mutating these interactions displays severe growth defects and eliminates association of eIF3i/TIF34 and strikingly also eIF3g/TIF35 with eIF3 and 40S subunits in vivo. Unexpectedly, 40S-association of the remaining eIF3 subcomplex and eIF5 is likewise destabilized resulting in formation of aberrant pre-initiation complexes (PICs) containing eIF2 and eIF1, which critically compromises scanning arrest on mRNA at its AUG start codon suggesting that the contacts between mRNA and ribosomal decoding site are impaired
Trvalý link: http://hdl.handle.net/11104/0210369