Evidence map›Paper›PMID 23867455›Full record

ArticleThe Journal of biological chemistry2013

Aminoacylating urzymes challenge the RNA world hypothesis.

Li Li, Christopher Francklyn, Charles W Carter

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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.

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3 · Its place in the literature

Who cites it

51 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Triplet-Encoded Prebiotic RNA Aminoacylation.Journal of the American Chemical Society · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Life in The Context of Order and Complexity.Life (Basel, Switzerland) · 2020
    Article
  19. Review
  20. 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

3 authors.

Li LiFrom the Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260 and.
Christopher Francklyn
Charles W Carter

Funding

Structure and Mechanism of Class II tRNA SynthetasesR01GM054899 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FRANCKLYN, CHRISTOPHER S · 1997 to 2017
$5.7M
Sense/Antisense Genetic Coding and the Origins of TranslationR01GM078227 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2006 to 2018
$3.9M
NIGMS NIH HHS R01 GM054899NIGMS NIH HHS R01 GM078227PHS HHS NIGMS 54899PHS HHS NIGMS 78227
6 · The paper itself

Abstract

We describe experimental evidence that ancestral peptide catalysts substantially accelerated development of genetic coding. Structurally invariant 120-130-residue Urzymes (Ur = primitive plus enzyme) derived from Class I and Class II aminoacyl-tRNA synthetases (aaRSs) acylate tRNA far faster than the uncatalyzed rate of nonribosomal peptide bond formation from activated amino acids. These new data allow us to demonstrate statistically indistinguishable catalytic profiles for Class I and II aaRSs in both amino acid activation and tRNA acylation, over a time period extending to well before the assembly of full-length enzymes and even further before the Last Universal Common Ancestor. Both Urzymes also exhibit ∼60% of the contemporary catalytic proficiencies. Moreover, they are linked by ancestral sense/antisense genetic coding, and their evident modularities suggest descent from even simpler ancestral pairs also coded by opposite strands of the same gene. Thus, aaRS Urzymes substantially pre-date modern aaRS but are, nevertheless, highly evolved. Their unexpectedly advanced catalytic repertoires, sense/antisense coding, and ancestral modularities imply considerable prior protein-tRNA co-evolution. Further, unlike ribozymes that motivated the RNA World hypothesis, Class I and II Urzyme·tRNA pairs represent consensus ancestral forms sufficient for codon-directed synthesis of nonrandom peptides. By tracing aaRS catalytic activities back to simpler ancestral peptides, we demonstrate key steps for a simpler and hence more probable peptide·RNA development of rapid coding systems matching amino acids with anticodon trinucleotides.

Indexed as

AminoacylationAmino Acyl-tRNA SynthetasesAnticodonCatalysisCatalytic DomainEvolution, MolecularGeobacillus stearothermophilusHumansModels, BiologicalNucleotidesPeptidesRhodopseudomonasRNA, TransferAmino Acyl-tRNA SynthetasesAnticodonNucleotidesPeptidesRNA, TransferAminoacyl tRNA SynthesisAminoacyl tRNA SynthetaseCatalytic RNAEnzyme CatalysisEnzyme ProficiencyMolecular EvolutionOrigin of TranslationProtein SynthesistRNA

Identifiers

PMID23867455
PMCPMC3772232

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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.