Evidence map›Paper›PMID 26160755›Full record

ArticleFEBS letters2015

A synthetic tRNA for EF-Tu mediated selenocysteine incorporation in vivo and in vitro.

Corwin Miller, Markus J Bröcker, Laure Prat, Kevan Ip, Napon Chirathivat, Alexander Feiock, Miklós Veszprémi, Dieter Söll

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 8% of its field
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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Tuning tRNAs for improved translation.Frontiers in genetics · 2024
    Review
  10. Review
  11. Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023
    Review
  12. Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023
    Article
  13. Creating Selenocysteine-Specific Reporters Using Inteins.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020
    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

8 authors at 1 institution in 1 country.

Corwin MillerDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. Electronic address: corwin.miller@yale.edu.
Markus J BröckerDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Laure PratDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Kevan IpDepartment 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.
Alexander FeiockDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Miklós VeszprémiDepartment 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; Department of Chemistry, Yale University, New Haven, CT 06520, USA. Electronic address: dieter.soll@yale.edu.
Yale University · US

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

Incorporation of selenocysteine (Sec) in bacteria requires a UGA codon that is reassigned to Sec by the Sec-specific elongation factor SelB and a conserved mRNA motif (SECIS element). These requirements severely restrict the engineering of selenoproteins. Earlier, a synthetic tRNASec was reported that allowed canonical Sec incorporation by EF-Tu; however, serine misincorporation limited its scope. We report a superior tRNASec variant (tRNAUTuX) that facilitates EF-Tu dependent stoichiometric Sec insertion in response to UAG both in vivo in Escherichia coli and in vitro in a cellfree protein synthesis system. We also demonstrate recoding of several sense codons in a SelB supplemented cell-free system. These advances in Sec incorporation will aid rational design and directed evolution of selenoproteins.

Indexed as

Protein BiosynthesisBacterial ProteinsBase SequenceCodon, TerminatorEscherichia coliMolecular Sequence DataMutationNucleic Acid ConformationPeptide Elongation FactorsPeptide Elongation Factor TuRNA, Transfer, Amino Acid-SpecificRNA, Transfer, Amino AcylSelenocysteineSelenoproteinsBacterial ProteinsCodon, TerminatorPeptide Elongation FactorsPeptide Elongation Factor TuRNA, Transfer, Amino Acid-SpecificRNA, Transfer, Amino AcylSelB protein, BacteriaSelenocysteineselenocysteinyl-tRNASelenoproteinstRNA, selenocysteine-Cell-free protein synthesisIn vitro translationNon-canonical amino acidSelenocysteineSelenoprotein

Identifiers

PMID26160755
PMCPMC4782793
OpenAlexW2121589924

What OpenQuestion holds

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Registered trials

None linked

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.