ArticleInternational journal of molecular sciences2015
The UGG Isoacceptor of tRNAPro Is Naturally Prone to Frameshifts.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 33 citations in OpenAlex.
- Discovery of 5‑Chlorotryptophan-Containing Antibiotics through Metabologenomics-Assisted High-Throughput Screening.JACS Au · 2025Article
- tRNA modifications as regulators of bacterial virulence and stress responses.PLoS pathogens · 2025Review
- Mechanistic Insights into SAM-Dependent Methyltransferases: A Review of Computational Approaches.International journal of molecular sciences · 2025Review
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.Nature communications · 2025Article
- Ribosomal frameshifting at normal codon repeats recodes functional chimeric proteins in human.Nucleic acids research · 2024Article
- Anticodon stem-loop tRNA modifications influence codon decoding and frame maintenance during translation.Seminars in cell & developmental biology · 2024Review
- Genome Expansion by tRNA +1 Frameshifting at Quadruplet Codons.Journal of molecular biology · 2022Review
- Interplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis.Nature communications · 2022Article
- Evolutionary repair reveals an unexpected role of the tRNA modification m1G37 in aminoacylation.Nucleic acids research · 2021Article
- Twice exploration of tRNA +1 frameshifting in an elongation cycle of protein synthesis.Nucleic acids research · 2021Article
- Loss ofeLife · 2021Article
- Adaptor Molecules Epitranscriptome Reprograms Bacterial Pathogenicity.International journal of molecular sciences · 2021Review
- Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation.Nature communications · 2021Article
- Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA.Nature communications · 2021Article
- Gene Expression Profiling ofFrontiers in microbiology · 2021Article
- tRNA methylation: An unexpected link to bacterial resistance and persistence to antibiotics and beyond.Wiley interdisciplinary reviews. RNA · 2020Review
- Article
- MgACS catalysis · 2020Article
- tRNA Methylation Is a Global Determinant of Bacterial Multi-drug Resistance.Cell systems · 2019Article
- AtTrm5a catalyses 1-methylguanosine and 1-methylinosine formation on tRNAs and is important for vegetative and reproductive growth in Arabidopsis thaliana.Nucleic acids research · 2019Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Native tRNAs often contain post-transcriptional modifications to the wobble position to expand the capacity of reading the genetic code. Some of these modifications, due to the ability to confer imperfect codon-anticodon pairing at the wobble position, can induce a high propensity for tRNA to shift into alternative reading frames. An example is the native UGG isoacceptor of E. coli tRNAPro whose wobble nucleotide U34 is post-transcriptionally modified to cmo5U34 to read all four proline codons (5'-CCA, 5'-CCC, 5'-CCG, and 5'-CCU). Because the pairing of the modified anticodon to CCC codon is particularly weak relative to CCA and CCG codons, this tRNA can readily shift into both the +1 and +2-frame on the slippery mRNA sequence CCC-CG. We show that the shift to the +2-frame is more dominant, driven by the higher stability of the codon-anticodon pairing at the wobble position. Kinetic analysis suggests that both types of shifts can occur during stalling of the tRNA in a post-translocation complex or during translocation from the A to the P-site. Importantly, while the +1-frame post complex is active for peptidyl transfer, the +2-frame complex is a poor peptidyl donor. Together with our recent work, we draw a mechanistic distinction between +1 and +2-frameshifts, showing that while the +1-shifts are suppressed by the additional post-transcriptionally modified m1G37 nucleotide in the anticodon loop, the +2-shifts are suppressed by the ribosome, supporting a role of the ribosome in the overall quality control of reading-frame maintenance.
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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.