ArticleThe EMBO journal1996
Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA(Ser) acceptor stem by E.coli seryl-tRNA synthetase.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 63 citations in OpenAlex.
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Prebiotic Assembly of Cloverleaf tRNA, Its Aminoacylation and the Origin of Coding, Inferred from Acceptor Stem Coding-Triplets.International journal of molecular sciences · 2022Article
- Biochemistry of Aminoacyl tRNA Synthetase and tRNAs and Their Engineering for Cell-Free and Synthetic Cell Applications.Frontiers in bioengineering and biotechnology · 2022Review
- Modulating Mistranslation Potential of tRNAGenetics · 2019Article
- Challenges of site-specific selenocysteine incorporation into proteins by Escherichia coli.RNA biology · 2018Review
- The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis.Nature reviews. Molecular cell biology · 2018Review
- Insights into substrate promiscuity of human seryl-tRNA synthetase.RNA (New York, N.Y.) · 2017Article
- Binding Properties of Split tRNA to the C-terminal Domain of Methionyl-tRNA Synthetase of Nanoarchaeum equitans.Journal of molecular evolution · 2017Article
- Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair.Journal of the American Chemical Society · 2016Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Origins and Early Evolution of the tRNA Molecule.Life (Basel, Switzerland) · 2015Review
- Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Revisiting the operational RNA code for amino acids: Ensemble attributes and their implications.RNA (New York, N.Y.) · 2010Article
- Efficient aminoacylation of the tRNA(Ala) acceptor stem: dependence on the 2:71 base pair.RNA (New York, N.Y.) · 2002Article
- Domain-domain communication in a miniature archaebacterial tRNA synthetase.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Correlation of deformability at a tRNA recognition site and aminoacylation specificity.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus.The EMBO journal · 1999Article
- Crystal structure of acceptor stem of tRNA(Ala) from Escherichia coli shows unique G.U wobble base pair at 1.16 A resolution.RNA (New York, N.Y.) · 1999Article
- The dual identities of mammalian tRNA(Sec) for SerRS and selenocysteine synthase.Molecular biology reports · 1998Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Aminoacylation rate determinations for a series of variant RNA minihelix substrates revealed that Escherichia coli seryl-tRNA synthetase (SerRS) recognizes the 1--72 through 5--68 base pairs of the E.coli tRNA(Ser) acceptor stem with the major recognition elements clustered between positions 2--71 and 4--69. The rank order of effects of canonical base pair substitutions at each position on kcat/Km was used to assess the involvement of major groove functional groups in recognition. Conclusions based on the biochemical data are largely consistent with the interactions revealed by the refined structure of the homologous Thermus thermophilus tRNA(Ser)-SerRS complex that Cusack and colleagues report in the accompanying paper. Disruption of an end-on hydrophobic interaction between the major groove C5(H) of pyrimidine 69 and an aromatic side chain of SerRS is shown to significantly decrease kcat/Km of a minihelix substrate. This type of interaction provides a means by which proteins can recognize the binary information of 'degenerate' sequences, such as the purine-pyrimidine base pairs of tRNA(Ser). The 3--70 base pair is shown to contribute to recognition by SerRS even though it is not contacted specifically by the protein. The latter effect derives from the organization of the specific contacts that SerRS makes with the neighboring 2--71 and 4--69 acceptor stem base pairs.
Indexed as
Identifiers
8654382PMC450222W2208605604What 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.