ArticleNucleic acids research2001
Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 151 citations in OpenAlex.
- Eukaryotic initiation factor eIF3 facilitates loading of eukaryotic release factor eRF1 or suppressor tRNA to the ribosome.Nucleic acids research · 2026Article
- Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome.Science (New York, N.Y.) · 2025Article
- Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation.Nucleic acids research · 2025Article
- Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024Article
- Two "Edges" in Our Knowledge on the Functions of Ribosomal Proteins: The Revealed Contributions of Their Regions to Translation Mechanisms and the Issues of Their Extracellular Transport by Exosomes.International journal of molecular sciences · 2023Review
- Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.Biochemistry. Biokhimiia · 2021Review
- The Halastavi árva Virus Intergenic Region IRES Promotes Translation by the Simplest Possible Initiation Mechanism.Cell reports · 2020Article
- CTELS: A Cell-Free System for the Analysis of Translation Termination Rate.Biomolecules · 2020Article
- The Origin and Evolution of Release Factors: Implications for Translation Termination, Ribosome Rescue, and Quality Control Pathways.International journal of molecular sciences · 2019Review
- Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1.Nature communications · 2018Article
- Article
- Cultured bloodstream Trypanosoma brucei adapt to life without mitochondrial translation release factor 1.Scientific reports · 2018Article
- RpbL12 Assists Catalysis by Correctly Positioning the Incoming Aminoacyl-tRNA in the A-Site ofThe open biochemistry journal · 2018Article
- RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.Nucleic acids research · 2017Article
- A Functional Role for the Monomethylated Gln-51 and Lys-53 Residues of the 49GGQTK53 Motif of eL42 from Human 80S Ribosomes.The open biochemistry journal · 2017Article
- Bacterial Protein Synthesis as a Target for Antibiotic Inhibition.Cold Spring Harbor perspectives in medicine · 2016Review
- Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.Scientific reports · 2016Article
- Non-Standard Genetic Codes Define New Concepts for Protein Engineering.Life (Basel, Switzerland) · 2015Review
- Adult Onset Leigh Syndrome in the Intensive Care Setting: A Novel Presentation of a C12orf65 Related Mitochondrial Disease.Journal of neuromuscular diseases · 2015Article
- Response to "Ribosome Rescue and Translation Termination at Non-standard Stop Codons by ICT1 in Mammalian Mitochondria".PLoS genetics · 2015Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previously, we have shown that all class-1 polypeptide release factors (RFs) share a common glycine-glycine-glutamine (GGQ) motif, which is critical for RF activity. Here, we subjected to site-directed mutagenesis two invariant amino acids, Gln185 and Arg189, situated in the GGQ minidomain of human eRF1, followed by determination of RF activity and the ribosome binding capacity for mutant eRF1. We show that replacement of Gln185 with polar amino acid residues causes partial inactivation of RF activity; Gln185Ile, Arg189Ala and Arg189Gln mutants are completely inactive; all mutants that retain partial RF activity respond similarly to three stop codons. We suggest that loss of RF activity for Gln185 and Arg189 mutants is caused by distortion of the conformation of the GGQ minidomain but not by damage of the stop codon recognition site of eRF1. Our data are inconsistent with the model postulating direct involvement of Gln185 side chain in orientation of water molecule toward peptidyl-tRNA ester bond at the ribosomal peptidyl transferase centre. Most of the Gln185 mutants exhibit reduced ability to bind to the ribosome, probably, to rRNA and/or (peptidyl)-tRNA(s). The data suggest that the GGQ motif is implicated both in promoting peptidyl-tRNA hydrolysis and binding to the ribosome.
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