ArticleThe EMBO journal1999
Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 80 citations in OpenAlex.
- Unexpected enzymatic function of an ancient nucleic acid-binding fold.Nucleic acids research · 2025Article
- Structural basis of tRNA recognition by the widespread OB fold.Nature communications · 2024Article
- Recognition of the tRNA structure: Everything everywhere but not all at once.Cell chemical biology · 2024Review
- Gain of C-Ala enables AlaRS to target the L-shaped tRNAAla.Nucleic acids research · 2022Article
- Identification of host tRNAs preferentially recognized by the Plasmodium surface protein tRip.Nucleic acids research · 2021Article
- RNA Aptamers for a tRNA-Binding Protein fromLife (Basel, Switzerland) · 2020Article
- Regulatory Factors for tRNA Modifications in Extreme- Thermophilic BacteriumFrontiers in genetics · 2019Review
- 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
- tRNA Modifications: Impact on Structure and Thermal Adaptation.Biomolecules · 2017Review
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Apicomplexa-specific tRip facilitates import of exogenous tRNAs into malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Architecture and metamorphosis.Topics in current chemistry · 2014Review
- A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes.Molecular and cellular biology · 2013Article
- A homology model for Clostridium difficile methionyl tRNA synthetase: active site analysis and docking interactions.Journal of molecular modeling · 2011Article
- An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions.The Journal of biological chemistry · 2011Article
- Arc1p is required for cytoplasmic confinement of synthetases and tRNA.Molecular and cellular biochemistry · 2007Article
- Association between Archaeal prolyl- and leucyl-tRNA synthetases enhances tRNA(Pro) aminoacylation.The Journal of biological chemistry · 2005Article
- Trbp111 selectively binds a noncovalently assembled tRNA-like structure.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The genome of the bacterium Aquifex aeolicus encodes a polypeptide which is related to a small portion of a sequence found in one prokaryotic and two eukaryotic tRNA synthetases. It also is related to a portion of Arc1p, a tRNA-binding protein believed to be important for nuclear trafficking of tRNAs. Here we cloned, expressed and purified the 111 amino acid polypeptide (designated Trbp111) and showed by ultracentrifugation analysis that it is a stable dimer in solution. The protein was also crystallized in a monoclinic lattice. X-ray diffraction analysis at 2.8 A resolution revealed a prominent non-crystallographic 2-fold axis, consistent with the presence of a symmetric homodimeric structure. Band-shift analysis with polyacrylamide gels showed that the dimer binds tRNAs, but not RNA duplexes, RNA hairpins, single-stranded RNA nor 5S rRNA. Complex formation with respect to tRNA is non-specific, with a single tRNA bound per dimer. Thus, Trbp111 is a structure-specific tRNA-binding protein. These results and other considerations raise the possibility that Trbp111 is a tRNA-specific chaperone which stabilizes the native L-shaped fold in the extreme thermophile and which has been incorporated into much larger tRNA-binding proteins of higher organisms.
Indexed as
Identifiers
What OpenQuestion holds
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.