ArticleJournal of molecular biology2016
Structural Basis for Translation Termination on a Pseudouridylated Stop Codon.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Functions and therapeutic applications of pseudouridylation.Nature reviews. Molecular cell biology · 2025Review
- "Goldilocks Modifications" for mRNA Therapeutics Won the Nobel Prize.Nucleic acid therapeutics · 2024Article
- Why U matters: detection and functions of pseudouridine modifications in mRNAs.Trends in biochemical sciences · 2024Review
- Review
- Chemical modifications to mRNA nucleobases impact translation elongation and termination.Biophysical chemistry · 2022Review
- A systematic dissection of determinants and consequences of snoRNA-guided pseudouridylation of human mRNA.Nucleic acids research · 2022Article
- A switch from α-helical to β-strand conformation during co-translational protein folding.The EMBO journal · 2022Article
- The Importance of the Epi-Transcriptome in Translation Fidelity.Non-coding RNA · 2021Review
- The epitranscriptome beyond mNature reviews. Genetics · 2021Review
- Regulation and Function of RNA Pseudouridylation in Human Cells.Annual review of genetics · 2020Review
- A molecular-level perspective on the frequency, distribution, and consequences of messenger RNA modifications.Wiley interdisciplinary reviews. RNA · 2020Review
- Pseudouridinylation of mRNA coding sequences alters translation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy.Nature communications · 2019Article
- Mechanism of premature translation termination on a sense codon.The Journal of biological chemistry · 2018Article
- Conformational Control of Translation Termination on the 70S Ribosome.Structure (London, England : 1993) · 2018Article
- Mechanism of Inhibition of Translation Termination by Blasticidin S.Journal of molecular biology · 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
- Position-dependent effects of regioisomeric methylated adenine and guanine ribonucleosides on translation.Nucleic acids research · 2017Article
- Ribosome rearrangements at the onset of translational bypassing.Science advances · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Pseudouridylation of messenger RNA emerges as an abundant modification involved in gene expression regulation. Pseudouridylation of stop codons in eukaryotic and bacterial cells results in stop-codon read through. The structural mechanism of this phenomenon is not known. Here we present a 3.1-Å crystal structure of Escherichia coli release factor 1 (RF1) bound to the 70S ribosome in response to the ΨAA codon. The structure reveals that recognition of a modified stop codon does not differ from that of a canonical stop codon. Our in vitro biochemical results support this finding by yielding nearly identical rates for peptide release from E. coli ribosomes programmed with pseudouridylated and canonical stop codons. The crystal structure also brings insight into E. coli RF1-specific interactions and suggests involvement of L27 in bacterial translation termination. Our results are consistent with a mechanism in which read through of a pseudouridylated stop codon in bacteria results from increased decoding by near-cognate tRNAs (miscoding) rather than from decreased efficiency of termination.
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Registered trials
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.