ArticleProceedings of the National Academy of Sciences of the United States of America2002
Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling.Nature communications · 2021Article
- Collateral Toxicity Limits the Evolution of Bacterial Release Factor 2 toward Total Omnipotence.Molecular biology and evolution · 2020Article
- Adaptive evolution of genomically recodedProceedings of the National Academy of Sciences of the United States of America · 2018Article
- R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteriaThe Journal of biological chemistry · 2017Article
- A genetic approach for analyzing the co-operative function of the tRNA mimicry complex, eRF1/eRF3, in translation termination on the ribosome.Nucleic acids research · 2014Article
- Article
- Evolution of molecular error rates and the consequences for evolvability.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Inactivation of the RluD pseudouridine synthase has minimal effects on growth and ribosome function in wild-type Escherichia coli and Salmonella enterica.Journal of bacteriology · 2011Article
- The codon specificity of eubacterial release factors is determined by the sequence and size of the recognition loop.RNA (New York, N.Y.) · 2010Article
- Principles of stop-codon reading on the ribosome.Nature · 2010Article
- Role of premature stop codons in bacterial evolution.Journal of bacteriology · 2008Article
- Mitochondrial release factor in yeast: interplay of functional domains.Current genetics · 2008Article
- Pseudouridylation of helix 69 of 23S rRNA is necessary for an effective translation termination.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Diverse bacterial genomes encode an operon of two genes, one of which is an unusual class-I release factor that potentially recognizes atypical mRNA signals other than normal stop codons.Biology direct · 2006Article
- Comparative study of translation termination sites and release factors (RF1 and RF2) in procaryotes.Journal of molecular evolution · 2003Article
- Stop codon selection in eukaryotic translation termination: comparison of the discriminating potential between human and ciliate eRF1s.The EMBO journal · 2003Article
- Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism of stop codon recognition during translation has long been a puzzle. Only recently has it been established that a tripeptide in the bacterial release factors (RFs) 1 and 2 serves as the "anticodon" in deciphering stop codons in mRNA. However, the molecular basis of the accuracy of stop codon recognition is unknown. Although specific tripeptides in the RFs are primarily responsible for selective reading of cognate stop codons, charge-flip variant RF proteins, altered at conserved Glu residues adjacent to the tripeptide-anticodon, are shown here to be crucial to codon recognition. Changes of these Glu residues are capable of triggering polypeptide release at noncognate stop codons and also at sense codons. These changes also reverse the growth inhibition by RFs containing "harmful" tripeptide-anticodon changes. These findings suggest that electrostatic interactions involving negative charges in domain C of the RFs mediate their accurate docking in the ribosome. Our results also establish that the charge flipping creates a phenotype/translation termination by "codon bypassing" via relaxed positioning of the RF tripeptide-anticodon in the decoding pocket of the ribosome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.