The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome.

By L. Passmore, T. Schmeing, David Maag, Drew Applefield, M. Acker, Mikkel A. Algire, J. Lorsch, V. Ramakrishnan. 2007

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In Molecular Biology

Citations in the corpus

The scanning mechanism of eukaryotic translation initiation. (2014, background): “The conformational rearrangement posited in this study probably corresponds to the switch from open to closed PIC conformations, which increases the stability of TC binding to reconstituted 43S/mRNA complexes on AUG recognition (186).”
Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation. (2017, background): “The PIN location of tRNAi in the py48S structure enables interactions of the ASL with rRNA residues in the P site, helping to account for the enhanced stability of the PIN state demonstrated biochemically [29,30].”
eIF5 and eIF5B together stimulate 48S initiation complex formation during ribosomal scanning (2014, background): “eIF1 and eIF1A together upon binding promote the rearrangement of the 40S subunit from a closed scanning-arrested to an open scanning-competent state (8).”
A structural inventory of native ribosomal ABCE1‐43S pre‐initiation complexes (2020, neutral): “The 40S in State I resembled the state of an empty 40S subunit with a closed latch (Heuer et al , 2017; Passmore et al , 2007), and only the core eIF3 subunits and weakly bound eIF1 were found.”
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets (2009, neutral): “It appears that eIF1 promotes scanning when nonAUG codons occupy the P-site by stabilizing an open conformation of the mRNA binding cleft of the 40S subunit, possibly by modulating the conformation of the “latch” to the mRNA entry channel (Passmore et al., 2007) (Figures 2A and 2B).”
Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2 (2020, background): “The C-terminus of Nsp1 is located close to the so called “latch” between the rRNA helix h18 of the body and h34 of the head of the 40S subunit, which influences mRNA accommodation and movement during translation initiation ( 22, 23 ).”
Structural Changes Enable Start Codon Recognition by the Eukaryotic Translation Initiation Complex (2014, background): “…from the pm43S (Hashem et al., 2013), in which tRNAi is not buried as deeply in the P site, would not clash with either conformation of eIF1 (Figure 5), consistent with the fact that eIF1 actually promotes TC binding in the POUT conformation (Passmore et al., 2007; Martin-Marcos et al., 2013).”
Toward a Kinetic Understanding of Eukaryotic Translation. (2018, background): “The binding of eIF1 and eIF1A to the 40S subunit generates this conformation (Pestova et al. 1998; Passmore et al. 2007; Hussain et al. 2014).”
THE MECHANISM OF EUKARYOTIC TRANSLATION INITIATION AND PRINCIPLES OF ITS REGULATION (2010, background): “Importantly, binding of eIF1 and eIF1A to 40S subunits induces conformational change”
eIF3j is located in the decoding center of the human 40S ribosomal subunit. (2007, background): “…A site and is thought to facilitate the recruitment of Met-tRNA i and direct it to the peptidyl (P) site (Carter et al., 2001; Fekete et al., 2005; Passmore et al., 2007). eIF1A also promotes correct recognition of the initiation codon in association with initiation factor eIF1 (Pestova et al.,…”
Protein Synthesis Initiation in Eukaryotic Cells. (2018, background): “Their cooperative binding induces conformational changes that rotate the head and open up a cleft between the head and body of the 40S to facilitate TC binding (Maag et al. 2005; Passmore et al. 2007; Weisser et al. 2013; Sokabe and Fraser 2014).”