Evidence map›Paper›PMID 26026160›Full record

ArticleNucleic acids research2015

Outwitting EF-Tu and the ribosome: translation with d-amino acids.

John Achenbach, Michael Jahnz, Lucas Bethge, Krisztina Paal, Maria Jung, Maja Schuster, Renate Albrecht, Florian Jarosch, Knud H Nierhaus, Sven Klussmann

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–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

35 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
  6. Article
  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. Article
  10. Article
  11. Tuning tRNAs for improved translation.Frontiers in genetics · 2024
    Review
  12. Ribosomal incorporation of negatively charged d-α- andPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Trends in peptide drug discovery.Nature reviews. Drug discovery · 2021
    Article
  17. Article
  18. Review
  19. Chiral checkpoints during protein biosynthesis.The Journal of biological chemistry · 2019
    Review
  20. Article
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

10 authors.

John AchenbachNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany jachenbach@noxxon.com.ORCID http://orcid.org/0000-0001-8161-4335
Michael JahnzNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.
Lucas BethgeNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.
Krisztina PaalNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.
Maria JungNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.
Maja SchusterNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.
Renate AlbrechtInstitut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Florian JaroschNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.
Knud H NierhausInstitut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany nierhaus@molgen.mpg.de.
Sven KlussmannNOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Key components of the translational apparatus, i.e. ribosomes, elongation factor EF-Tu and most aminoacyl-tRNA synthetases, are stereoselective and prevent incorporation of d-amino acids (d-aa) into polypeptides. The rare appearance of d-aa in natural polypeptides arises from post-translational modifications or non-ribosomal synthesis. We introduce an in vitro translation system that enables single incorporation of 17 out of 18 tested d-aa into a polypeptide; incorporation of two or three successive d-aa was also observed in several cases. The system consists of wild-type components and d-aa are introduced via artificially charged, unmodified tRNA(Gly) that was selected according to the rules of 'thermodynamic compensation'. The results reveal an unexpected plasticity of the ribosomal peptidyltransferase center and thus shed new light on the mechanism of chiral discrimination during translation. Furthermore, ribosomal incorporation of d-aa into polypeptides may greatly expand the armamentarium of in vitro translation towards the identification of peptides and proteins with new properties and functions.

Indexed as

Peptide BiosynthesisAmino AcidsPeptide Elongation Factor TuPeptidesRibosomesRNA, TransferRNA, Transfer, Amino AcylStereoisomerismTransfer RNA AminoacylationAmino AcidsPeptide Elongation Factor TuPeptidesRNA, TransferRNA, Transfer, Amino Acyl

Identifiers

PMID26026160
PMCPMC4499158

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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.