Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase

@article{Jahn1991AnticodonAA,
  title={Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase},
  author={Martina Jahn and Michael J. Rogers and Dieter S{\"o}ll},
  journal={Nature},
  year={1991},
  volume={352},
  pages={258-260}
}
THE correct attachment of amino acids to their corresponding (cognate) transfer RNA catalysed by aminoacyl-tRNA synthetases is a key factor in ensuring the fidelity of protein biosynthesis. Previous studies have demonstrated that the interaction of Escherichia coli tRNAGln with glutaminyl-tRNA synthetase (GlnRS) provides an excellent system1 to study this highly specific recognition process, also referred to as 'tRNA identity'2. Accurate acylation of tRNA depends mainly on two principles: a set… 
Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase.
TLDR
A more extensive mutational analysis shows the importance of the acceptor binding domain to accurate recognition of tRNA and the structure of the GlnRS complex supports studies from amber and opal suppressor tRNAs.
Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.
TLDR
It is shown that, during the complex formation, aminoacyl-tRNA synthetases are at least partially responsible for conformational changes which involve structural constraints in tRNA molecules.
The Role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases
SummaryThe T7 polymerase transcription system was used for in vitro synthesis of unmodified versions of the E. coli tRNA mutants that insert asparagine, cysteine, glycine, histidine, and serine.
Structure of Escherichia coli Arginyl-tRNA Synthetase in Complex with tRNAArg: Pivotal Role of the D-loop.
TLDR
Structural and functional data indicate that the unprecedented ArgRS crystal structure represents a snapshot during functioning and suggest that the recognition of the D-loop by ArgRS is an important trigger that anchors tRNAArg on the synthetase.
Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.
TLDR
An important role for surrounding nucleotides in maintaining the integrity of the tertiary core and its consequent ability to present crucial recognition determinants to aminoacyl-tRNA synthetases is implicated.
Transfer RNA‐dependent cognate amino acid recognition by an aminoacyl‐tRNA synthetase.
TLDR
The observed role of RNA as a cofactor in optimizing amino acid activation suggests that the tRNAGln‐GlnRS complex may be partly analogous to ribonucleoprotein enzymes where protein‐RNA interactions facilitate catalysis.
Enzymatic aminoacylation of tRNA acceptor stem helices with cysteine is dependent on a single nucleotide.
TLDR
A dominant role of U73 is demonstrated for aminoacylation of small RNA helices by cysteine tRNA synthetase of Escherichia coli tRNA(Cys) with high catalytic efficiency.
The influence of identity elements on the aminoacylation of tRNAArg by plant and Escherichia coli arginyl‐tRNA synthetases
TLDR
In-vitro tRNA transcripts are designed, based on the soybean tRNAArg primary structure, aiming to investigate its specific aminoacylation by two recombinant plant arginyl‐tRNA synthetases and to compare this with the enzyme from E. coli.
Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity.
TLDR
The kinetic evaluation of the anticodon switch mutants suggests that overlap in anticodon recognition is avoided through specificity for the third anticodon position coupled with divergent preferences for the wobble base, suggesting that tRNA(Glu) contains antideterminants to glutamine identity.
Recognition in the Glutamine tRNA System: from Structure to Function
TLDR
This chapter focuses on the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase (GlnRS), arguably the best characterized aaRS-t RNA interaction both functionally and structurally, as the first high-resolution crystal structure of a protein-RNA complex was solved for GlnRS:tRNAGln.
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TLDR
Treatment of unfractionated Escherichia coli tRNA with BrCN produces a decrease in glutamine and glutamate acceptance, which suggests that the presence of the 2-thiouridine derivative itself in the anticodon of the tRNA is not a necessary requirement for the specific interaction with cognate aminoacyl-tRNA synthetase.
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TLDR
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TLDR
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TLDR
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    Proceedings of the National Academy of Sciences of the United States of America
  • 1988
TLDR
Analysis of the in vivo amber suppressor activity of mutants derived from two Escherichia coli serine tRNAs shows that substitution of 2 base pairs in the acceptor helix changes a serine suppressor tRNA to an efficient glutamine acceptor, implying that misaminoacylation in vivo is dependent on the competition by different synthetases for the tRNA.
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TLDR
In vitro aminoacylation reactions with purified GlnS7 protein show that this enzyme can also mischarge some tRNA species lacking the amber anticodon, an example of mischarging phenotype conferred by a mutation in an aminoacyl-tRNA synthetase gene.
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TLDR
These genetic experiments define two positions in GlnRS where amino acid substitution results in a relaxed specificity of tRNA discrimination, and identify specific areas in the structure of theGlnRS:tRNA(Gln) complex that are critical to accurate t RNA discrimination by Gln RS.
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