Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit

By J. M. Ogle, D. Brodersen, W. M. Clemons, M. Tarry, A. Carter, V. Ramakrishnan. Science, 2001

1,211 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3bafe970869aeeed8fbc5cb75c5cc41e1cdba734

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In Molecular Biology

1. C. Fraser
2. C. Hellen
3. A. Hinnebusch
4. Neocles Leontis
5. W. Merrick
6. Eric Westhof
7. A. Pisarev
8. V. Pisareva

Citations in the corpus

• GTP hydrolysis by IF2 guides progression of the ribosome into elongation (2009, background): “These labeling sites are distant from the binding sites of IF1, IF2, and IF3, the ribosomal sites responsible for GTPase stimulation, and dynamic domains, such as the 30S head and 50S L1 and L7/L12 stalk regions (Figure 1) (Carter et al., 2001; Allen et al., 2005; Myasnikov et al., 2005; Dallas and ”
• eIF3j is located in the decoding center of the human 40S ribosomal subunit. (2007, methodology): “This enabled modeling of the C-terminal amino acid positions of eIF3j onto the crystal structure of the T. thermophilus 30S subunit (Ogle et al., 2001).”
• An RNA-centric historical narrative around the Protein Data Bank (2021, background): “Prevalence of A-minor contacts (193); A-minor recognition of codon/anticodon triplet (194), base–phosphate contacts (195), conservation of GoU pairs (196), multiple junctions (197)”
• Versatility of Aminoglycosides and Prospects for Their Future (2003, background): “The structure of the 30S subunit indicates that two universally conserved adenine residues (A1492 and A1493) are directly involved in the decoding process during normal translation (213).”
• The spliceosome: design principles of a dynamic RNP machine. (2009, background): “Structural (Ogle et al., 2001; Selmer et al., 2006; Simonovic and Steitz, 2008) and kinetic studies (Wohlgemuth et al.”
• Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes (2016, background): “Cognate codon-anticodon recognition in the decoding center of bacterial ribosomes induces a subtle but large-scale conformational change in the small subunit (SSU), referred to as domain closure (Ogle et al., 2001, 2002) (Figure 4A).”
• Studies on the role of helix 69 of 23S rRNA in the factor-dependent stages of translation initiation, elongation, and termination (2011, background): “A similar flipping-out of A1492 and A1493 during elongator aminoacyl-tRNA binding to the ribosomal A-site is known to induce a large-scale conformational rearrangement in the 30S subunit (Ogle et al. 2001).”
• 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, methodology): “…(AA1492–1493 in T. Thermophilus) flip out upon binding of cognate aminoacyl tRNA to the A-site during elongation and interact with the minor groove of the first two base pairs of the base-paired codon–anticodon helix, thereby monitoring the fidelity of elongator tRNA selection (Ogle et al. 2001).”
• Aminoglycoside Modifying Enzymes (2010, background): “It is clear now that pairing of the codon/anticodon nucleotides cannot account for the levels of fidelity observed in selection of the correct aminoacyl-tRNA (Ogle et al., 2001; Ogle et al., 2003).”