Evidence map›Paper›PMID 38783009›Full record

ArticleNucleic acids research2024

Primordial aminoacyl-tRNA synthetases preferred minihelices to full-length tRNA.

Guo Qing Tang, Hao Hu, Jordan Douglas, Charles W Carter

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. The central dogma in reverse.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

4 authors.

Guo Qing TangDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.
Hao HuDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.
Jordan DouglasDepartment of Physics, The University of Auckland, New Zealand.ORCID 0000-0003-0371-9961
Charles W CarterDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.ORCID 0000-0002-2653-4452

Funding

Alfred P. Sloan Foundation Matter-to-Life program G-2021-16944
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (AARS) and tRNAs translate the genetic code in all living cells. Little is known about how their molecular ancestors began to enforce the coding rules for the expression of their own genes. Schimmel et al. proposed in 1993 that AARS catalytic domains began by reading an 'operational' code in the acceptor stems of tRNA minihelices. We show here that the enzymology of an AARS urzyme•TΨC-minihelix cognate pair is a rich in vitro realization of that idea. The TΨC-minihelixLeu is a very poor substrate for full-length Leucyl-tRNA synthetase. It is a superior RNA substrate for the corresponding urzyme, LeuAC. LeuAC active-site mutations shift the choice of both amino acid and RNA substrates. AARS urzyme•minihelix cognate pairs are thus small, pliant models for the ancestral decoding hardware. They are thus an ideal platform for detailed experimental study of the operational RNA code.

Indexed as

Amino Acyl-tRNA SynthetasesNucleic Acid ConformationRNA, TransferCatalytic DomainGenetic CodeLeucine-tRNA LigaseRNA, CatalyticSubstrate SpecificityAmino Acyl-tRNA SynthetasesLeucine-tRNA LigaseRNA, CatalyticRNA, Transfer

Identifiers

PMID38783009
PMCPMC11229368

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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.