Archaeal translation initiation factor aIF2 can substitute for eukaryotic eIF2 in ribosomal scanning during mammalian 48S complex formationстатья
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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Аннотация:Heterotrimeric translation initiation factor (IF) a/eIF2 (archaeal/eukaryotic IF
2) is present in both Eukarya and Archaea. Despite strong structural similarity
between a/eIF2 orthologs from the two domains of life, their functional
relationship is obscure. Here, we show that aIF2 from Sulfolobus solfataricus can
substitute for its mammalian counterpart in the reconstitution of eukaryotic 48S
initiation complexes from purified components. aIF2 is able to correctly place
the initiator Met-tRNA(i) into the P-site of the 40S ribosomal subunit and
accompany the entire set of eukaryotic translation IFs in the process of
cap-dependent scanning and AUG codon selection. However, it seems to be unable to
participate in the following step of ribosomal subunit joining. In accordance
with this, aIF2 inhibits rather than stimulates protein synthesis in mammalian
cell-free system. The ability of recombinant aIF2 protein to direct ribosomal
scanning suggests that some archaeal mRNAs may utilize this mechanism during
translation initiation.