ArticleNucleic acids research2015
Stabilization of eukaryotic ribosomal termination complexes by deacylated tRNA.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- The ABCF ATPase New1 resolves translation termination defects associated with specific tRNAArg and tRNALys isoacceptors in the P site.Nucleic acids research · 2024Article
- The ABCF ATPase New1 resolves translation termination defects associated with specific tRNAbioRxiv : the preprint server for biology · 2024Article
- Humans and other commonly used model organisms are resistant to cycloheximide-mediated biases in ribosome profiling experiments.Nature communications · 2021Article
- Two alternative conformations of mRNA in the human ribosome during elongation and termination of translation as revealed by EPR spectroscopy.Computational and structural biotechnology journal · 2021Article
- A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling.Nucleic acids research · 2019Article
- Polyadenylate-binding protein-interacting proteins PAIP1 and PAIP2 affect translation termination.The Journal of biological chemistry · 2019Article
- Eukaryotic translation elongation factor 2 (eEF2) catalyzes reverse translocation of the eukaryotic ribosome.The Journal of biological chemistry · 2018Article
- RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.Nucleic acids research · 2017Article
- PABP enhances release factor recruitment and stop codon recognition during translation termination.Nucleic acids research · 2016Article
- Centers of motion associated with EF-Tu binding to the ribosome.RNA biology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stabilization of the ribosomal complexes plays an important role in translational control. Mechanisms of ribosome stabilization have been studied in detail for initiation and elongation of eukaryotic translation, but almost nothing is known about stabilization of eukaryotic termination ribosomal complexes. Here, we present one of the mechanisms of fine-tuning of the translation termination process in eukaryotes. We show that certain deacylated tRNAs, remaining in the E site of the ribosome at the end of the elongation cycle, increase the stability of the termination and posttermination complexes. Moreover, only the part of eRF1 recognizing the stop codon is stabilized in the A site of the ribosome, and the stabilization is not dependent on the hydrolysis of peptidyl-tRNA. The determinants, defining this property of the tRNA, reside in the acceptor stem. It was demonstrated by site-directed mutagenesis of tRNA(Val) and construction of a mini-helix structure identical to the acceptor stem of tRNA. The mechanism of this stabilization is different from the fixation of the unrotated state of the ribosome by CCA end of tRNA or by cycloheximide in the E site. Our data allow to reveal the possible functions of the isodecoder tRNAs in eukaryotes.
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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.