ArticleProceedings of the National Academy of Sciences of the United States of America1998
Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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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Who cites it
35 citing papers in PubMed, 77 citations in OpenAlex.
- Collateral Toxicity Limits the Evolution of Bacterial Release Factor 2 toward Total Omnipotence.Molecular biology and evolution · 2020Article
- Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Proceedings 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
- Rewriting the Genetic Code.Annual review of microbiology · 2017Review
- Functional Constraints on Replacing an Essential Gene with Its Ancient and Modern Homologs.mBio · 2017Article
- Experimental Evolution of Escherichia coli Harboring an Ancient Translation Protein.Journal of molecular evolution · 2017Article
- Overcoming Challenges in Engineering the Genetic Code.Journal of molecular biology · 2016Review
- Peptide release promoted by methylated RF2 and ArfA in nonstop translation is achieved by an induced-fit mechanism.RNA (New York, N.Y.) · 2016Article
- Highly reproductive Escherichia coli cells with no specific assignment to the UAG codon.Scientific reports · 2015Article
- 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
- Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.FEBS letters · 2012Article
- Release factor one is nonessential in Escherichia coli.ACS chemical biology · 2012Article
- Efficient decoding of the UAG triplet as a full-fledged sense codon enhances the growth of a prfA-deficient strain of Escherichia coli.Journal of bacteriology · 2012Article
- RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites.Nature chemical biology · 2011Article
- Structural aspects of translation termination on the ribosome.RNA (New York, N.Y.) · 2011Review
- The codon specificity of eubacterial release factors is determined by the sequence and size of the recognition loop.RNA (New York, N.Y.) · 2010Article
- Review
- Enhancement of the synthesis of RpoE and StpA by polyamines at the level of translation in escherichia coli under heat shock conditions.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prokaryotic translational release factors, RF1 and RF2, catalyze polypeptide release at UAG/UAA and UGA/UAA stop codons, respectively. In this study, we isolated a bacterial RF2 mutant (RF2*) containing an E167K substitution that restored the growth of a temperature-sensitive RF1 strain of Escherichia coli and the viability of a chromosomal RF1/RF2 double knockout. In both in vivo and in vitro polypeptide termination assays, RF2* catalyzed UAG/UAA termination, as does RF1, as well as UGA termination, showing that RF2* acquired omnipotent release activity. This result suggests that the E167K mutation abolished the putative third-base discriminator function of RF2. These findings are interpreted as indicating that prokaryotic and eukaryotic release factors share the same anticodon moiety and that only one omnipotent release factor is sufficient for bacterial growth, similar to the eukaryotic single omnipotent factor.
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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.