Evidence map›Paper›PMID 24890918›Full record

ArticleChembiochem : a European journal of chemical biology2014

Exploring the substrate range of wild-type aminoacyl-tRNA synthetases.

Chenguang Fan, Joanne M L Ho, Napon Chirathivat, Dieter Söll, Yane-Shih Wang

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.Chembiochem : a European journal of chemical biology · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Upgrading aminoacyl-tRNA synthetases for genetic code expansion.Current opinion in chemical biology · 2018
    Review
  15. Engineering posttranslational proofreading to discriminate nonstandard amino acids.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Rewiring protein synthesis: From natural to synthetic amino acids.Biochimica et biophysica acta. General subjects · 2017
    Review
  18. Article
  19. Article
  20. Rewriting the Genetic Code.Annual review of microbiology · 2017
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Chenguang Fan *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 (USA).
Joanne M L Ho *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 (USA).
Napon ChirathivatDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 (USA).
Dieter SöllDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 (USA).
Yane-Shih WangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520 (USA).

Funding

TRANSFER RNAR01GM022854 · NIGMS · YALE UNIVERSITY · PI SOLL, DIETER · 1985 to 2016
$21.3M
TRANSFER RNAR37GM022854 · NIGMS · YALE UNIVERSITY · PI SOLL, DIETER G · 1991 to 2000
$786k
NIGMS NIH HHS GM22854NIGMS NIH HHS R01 GM022854NIGMS NIH HHS R37 GM022854
6 · The paper itself

Abstract

We tested the substrate range of four wild-type E. coli aminoacyl-tRNA synthetases (AARSs) with a library of nonstandard amino acids (nsAAs). Although these AARSs could discriminate efficiently against the other canonical amino acids, they were able to use many nsAAs as substrates. Our results also show that E. coli tryptophanyl-tRNA synthetase (TrpRS) and tyrosyl-tRNA synthetase have overlapping substrate ranges. In addition, we found that the nature of the anticodon sequence of tRNA(Trp) altered the nsAA substrate range of TrpRS; this implies that the sequence of the anticodon affects the TrpRS amino acid binding pocket. These results highlight again that inherent AARS polyspecificity will be a major challenge in the aim of incorporating multiple different amino acids site-specifically into proteins.

Indexed as

Amino AcidsAmino Acyl-tRNA SynthetasesAnticodonEscherichia coliMolecular ConformationSubstrate SpecificityAmino AcidsAmino Acyl-tRNA SynthetasesAnticodonaminoacyl-tRNA synthetasesnatural nonsense tRNA suppressorsnonstandard amino acidssubstrate specificitysynthetic biologytRNA

Identifiers

PMID24890918
PMCPMC4133344

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Registered trials

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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.