ArticleProceedings of the National Academy of Sciences of the United States of America2002
Trbp111 selectively binds a noncovalently assembled tRNA-like structure.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Unexpected enzymatic function of an ancient nucleic acid-binding fold.Nucleic acids research · 2025Article
- Recognition of the tRNA structure: Everything everywhere but not all at once.Cell chemical biology · 2024Review
- Combinatorial Fusion Rules to Describe Codon Assignment in the Standard Genetic Code.Life (Basel, Switzerland) · 2020Article
- RNA Aptamers for a tRNA-Binding Protein fromLife (Basel, Switzerland) · 2020Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis.Nature reviews. Molecular cell biology · 2018Review
- Binding Properties of Split tRNA to the C-terminal Domain of Methionyl-tRNA Synthetase of Nanoarchaeum equitans.Journal of molecular evolution · 2017Article
- Bridging the gap between ribosomal and nonribosomal protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Transfer RNAs are key components of the genetic code by virtue of aminoacylation reactions whereby each amino acid is linked to the tRNA that bears the anticodon for the attached amino acid. The L-shaped tRNA structure contains two domains connected at right angles through a corner formed from tertiary interactions involving loops of each domain. Some evidence suggests that the domains arose separately and eventually were fused into a single covalent structure. In this scenario, the present-day tRNA possibly developed through a noncovalently assembled heterodimeric intermediate. Trbp111 is an ancient structure-specific tRNA binding protein that interacts specifically with the outside corner of the L-shaped molecule. Plausibly, this protein could act as a chaperone to cover and protect the fragile corner and thereby have a historical role in the development of tRNA. Here we show that Trbp111 interacts with a noncovalently assembled tRNA-like structure, under conditions where it does not interact with individual tRNA domains. Trbp111 binding specifically requires formation of the tRNA-like corner. In a mixture of RNA domains, it selects those that can make the L-like structure. Thus, cofactors such as Trbp111 have the capacity to help assemble and stabilize RNA dimers that are tRNA-like.
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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.