GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2.

By Lee D Kapp, J. Lorsch. 2004

159 citations recorded by the source corpus.

Subfields: Molecular Biology

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In Molecular Biology

1. A. Hinnebusch
2. I. S. Fernández
3. M. Sokabe
4. C. Fraser
5. W. Merrick
6. G. Pavitt
7. C. Hellen
8. J. Lorsch

Citations in the corpus

• The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit (2011, background): “Under our conditions, eIF2–GDPNP alone binds Met-tRNAi with a dissociation constant of 35±2nM, which is in good agreement with a previously reported value with the rabbit factor (28–47 nM) (17) and is slightly weaker than that of yeast eIF2 (10 nM) (19).”
• Molecular architecture of a eukaryotic translational initiation complex (2013, background): “It is known that the A1-U72 base pair is an essential discriminating feature of initiator tRNA (24).”
• The scanning mechanism of eukaryotic translation initiation. (2014, background): “The first base pair of the tRNAi acceptor (Acc) stem, A1:U72, enhances Met-tRNAi binding to eIF2-GTP (24, 26) and, together with contributions from G31:C39 in the anticodon stem loop (ASL) and residues A54 and A60 in the T loop, confers eIF2 specificity for initiator versus elongator Met-tRNA (27, 2”
• THE MECHANISM OF EUKARYOTIC TRANSLATION INITIATION AND PRINCIPLES OF ITS REGULATION (2010, background): “GTP hydrolysis reduces eIF2's affinity for Met-tRNA Met i , leading to partial dissociation of eIF2–GDP from 40S subunit”
• The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. (2007, methodology): “and purified as described ( Kapp and Lorsch [2004a] and Lorsch and Herschlag [1999], respectively).”
• Protein Synthesis Initiation in Eukaryotic Cells. (2018, background): “Met-tRNAi is brought to the ribosome in a complex with eIF2•GTP. eIF2 is a GDP/GTP binding “G” protein and has high affinity for Met-tRNAi only when GTP-bound (Kapp and Lorsch 2004).”
• Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. (2006, background): “Consistent with the affinities to Met-tRNAMeti of eIF2-GTP and eIF2-GDP differing by only one order of magnitude (Kapp and Lorsch 2004), in the absence of sucrose density gradient centrifugation, eIF5-induced hydrolysis of eIF2-bound GTP did not lead to complete dissociation of eIF2 from 48S…”