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

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

  • J Biol Chem. 2010 Aug 27;285(35):26779-26787. doi: 10.1074/jbc.M110.119693.
Sergey E Dmitriev 1 Ilya M Terenin 1 Dmitri E Andreev 1 Pavel A Ivanov 2 Jacov E Dunaevsky 1 William C Merrick 3 Ivan N Shatsky 4
Affiliations

Affiliations

  • 1 Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
  • 2 Faculty of Biology, Moscow State University, Moscow 119992, Russia.
  • 3 Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
  • 4 Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. Electronic address: shatsky@genebee.msu.su.
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.

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