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GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor.


ABSTRACT: During translation, aminoacyl-tRNAs are delivered to the ribosome by specialized GTPases called translation factors. Here, we report the tRNA binding to the P-site of 40 S ribosomes by a novel GTP-independent factor eIF2D isolated from mammalian cells. The binding of tRNA(i)(Met) occurs after the AUG codon finds its position in the P-site of 40 S ribosomes, the situation that takes place during initiation complex formation on the hepatitis C virus internal ribosome entry site or on some other specific RNAs (leaderless mRNA and A-rich mRNAs with relaxed scanning dependence). Its activity in tRNA binding with 40 S subunits does not require the presence of the aminoacyl moiety. Moreover, the factor possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40 S subunit. The corresponding gene is found in all eukaryotes and includes an SUI1 domain present also in translation initiation factor eIF1. The versatility of translation initiation strategies in eukaryotes is discussed.

SUBMITTER: Dmitriev SE 

PROVIDER: S-EPMC2930676 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor.

Dmitriev Sergey E SE   Terenin Ilya M IM   Andreev Dmitri E DE   Ivanov Pavel A PA   Dunaevsky Jacov E JE   Merrick William C WC   Shatsky Ivan N IN  

The Journal of biological chemistry 20100621 35


During translation, aminoacyl-tRNAs are delivered to the ribosome by specialized GTPases called translation factors. Here, we report the tRNA binding to the P-site of 40 S ribosomes by a novel GTP-independent factor eIF2D isolated from mammalian cells. The binding of tRNA(i)(Met) occurs after the AUG codon finds its position in the P-site of 40 S ribosomes, the situation that takes place during initiation complex formation on the hepatitis C virus internal ribosome entry site or on some other sp  ...[more]

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