ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural basis for functional mimicry of long-variable-arm tRNA by transfer-messenger RNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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60 citing papers in PubMed, 109 citations in OpenAlex.
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- Bacterial Ribosome Rescue Systems.Microorganisms · 2022Review
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- Structures of tmRNA and SmpB as they transit through the ribosome.Nature communications · 2021Article
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- Rational Design of Aptamer-Tagged tRNAs.International journal of molecular sciences · 2020Article
- TRMT2B is responsible for both tRNA and rRNA mRNA biology · 2020Article
- How a circularized tmRNA moves through the ribosome.Science (New York, N.Y.) · 2019Article
- Structural Basis for tRNA Mimicry by a Bacterial Y RNA.Structure (London, England : 1993) · 2018Article
- Numerical integration methods and layout improvements in the context of dynamic RNA visualization.BMC bioinformatics · 2017Article
- Ribosome-based quality control of mRNA and nascent peptides.Wiley interdisciplinary reviews. RNA · 2017Review
- mRNA modifications: Dynamic regulators of gene expression?RNA biology · 2016Review
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Article
- HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.Molecular cell · 2015Article
- Mechanisms of ribosome rescue in bacteria.Nature reviews. Microbiology · 2015Review
- The tmRNA website.Nucleic acids research · 2015Article
- The bacterial translation stress response.FEMS microbiology reviews · 2014Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
tmRNA and small protein B (SmpB) are essential trans-translation system components. In the present study, we determined the crystal structure of SmpB in complex with the entire tRNA domain of the tmRNA from Thermus thermophilus. Overall, the ribonucleoprotein complex (tRNP) mimics a long-variable-arm tRNA (class II tRNA) in the canonical L-shaped tertiary structure. The tmRNA terminus corresponds to the acceptor and T arms, or the upper part, of tRNA. On the other hand, the SmpB protein simulates the lower part, the anticodon and D stems, of tRNA. Intriguingly, several amino acid residues collaborate with tmRNA bases to reproduce the canonical tRNA core layers. The linker helix of tmRNA had been considered to correspond to the anticodon stem, but the complex structure unambiguously shows that it corresponds to the tRNA variable arm. The tmRNA linker helix, as well as the long variable arm of class II tRNA, may occupy the gap between the large and small ribosomal subunits. This suggested how the tRNA domain is connected to the mRNA domain entering the mRNA channel. A loop of SmpB in the tRNP is likely to participate in the interaction with alanyl-tRNA synthetase, which may be the mechanism for the promotion of tmRNA alanylation by the SmpB protein. Therefore, the tRNP may simulate a tRNA, both structurally and functionally, with respect to aminoacylation and ribosome entry.
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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.