ArticleProceedings of the National Academy of Sciences of the United States of America2008
Shine-Dalgarno interaction prevents incorporation of noncognate amino acids at the codon following the AUG.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Adenine Enrichment at the Fourth CDS Residue in Bacterial Genes Is Consistent with Error Proofing for +1 Frameshifts.Molecular biology and evolution · 2017Article
- 70S-scanning initiation is a novel and frequent initiation mode of ribosomal translation in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The integrity of the G2421-C2395 base pair in the ribosomal E-site is crucial for protein synthesis.RNA biology · 2015Article
- Impact of P-Site tRNA and antibiotics on ribosome mediated protein folding: studies using the Escherichia coli ribosome.PloS one · 2014Article
- Problems with the Analyses of the Ribosomal Allosteric Three-site Model.The Journal of biological chemistry · 2012Article
- Further in vitro exploration fails to support the allosteric three-site model.The Journal of biological chemistry · 2012Article
- Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Navigating the ribosome's metastable energy landscape.Trends in biochemical sciences · 2009Review
- When starting over makes more sense.ACS chemical biology · 2009Article
- Review
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
During translation, usually only one in approximately 400 misincorporations affects the function of a nascent protein, because only chemically similar near-cognate amino acids are misincorporated in place of the cognate one. The deleterious misincorporation of a chemically dissimilar noncognate amino acid during the selection process is precluded by the presence of a tRNA at the ribosomal E-site. However, the selection of first aminoacyl-tRNA, directly after initiation, occurs without an occupied E-site, i.e., when only the P-site is filled with the initiator tRNA and thus should be highly error-prone. Here, we show how bacterial ribosomes have solved this accuracy problem: In the absence of a Shine-Dalgarno (SD) sequence, the first decoding step at the A-site after initiation is extremely error-prone, even resulting in the significant incorporation of noncognate amino acids. In contrast, when a SD sequence is present, the incorporation of noncognate amino acids is not observed. This is precisely the effect that the presence of a cognate tRNA at the E-site has during the elongation phase. These findings suggest that during the initiation phase, the SD interaction functionally compensates for the lack of codon-anticodon interaction at the E-site by reducing the misincorporation of near-cognate amino acids and prevents noncognate misincorporation.
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