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- W2135211598 abstract "Faithful decoding of the genetic information by the ribosome relies on kinetically driven mechanisms that promote selection of cognate substrates during elongation. Recently, we have shown that in addition to these kinetically driven mechanisms, the ribosome possesses a post peptidyl transfer quality control system that retrospectively monitors the codon–anticodon interaction in the P site, triggering substantial losses in the specificity of the A site during subsequent tRNA and RF selection when a mistake has occurred. Here, we report a detailed kinetic analysis of tRNA selection in the context of a mismatched P-site codon:anticodon interaction. We observe pleiotropic effects of a P-site mismatch on tRNA selection, such that near-cognate tRNA is processed by the ribosome almost as efficiently as cognate. In particular, after a miscoding event, near-cognate codon–anticodon complexes are stabilized on the ribosome to an extent similar to that observed for cognate ones. Moreover, the two observed forward rates of GTPase activation and accommodation are greatly accelerated (∼10-fold) for near-cognate tRNAs. Because the ensemble of effects of a mismatched P site on substrate selection were found to be different from those reported for other ribosomal perturbations and miscoding agents, we propose that the structural integrity of the mRNA–tRNA helix in the P site provides a distinct molecular switch that dictates the specificity of the A site." @default.
- W2135211598 created "2016-06-24" @default.
- W2135211598 creator A5050772561 @default.
- W2135211598 creator A5070394026 @default.
- W2135211598 date "2010-08-19" @default.
- W2135211598 modified "2023-09-25" @default.
- W2135211598 title "Kinetic basis for global loss of fidelity arising from mismatches in the P-site codon:anticodon helix" @default.
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- W2135211598 doi "https://doi.org/10.1261/rna.2241810" @default.
- W2135211598 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2941106" @default.
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