Evidence map›Paper›PMID 17110438›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Emergence of the universal genetic code imprinted in an RNA record.

Michael J Hohn, Hee-Sung Park, Patrick O'Donoghue, Michael Schnitzbauer, Dieter Söll

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

42 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. "Not-so-popular" orthogonal pairs in genetic code expansion.Protein science : a publication of the Protein Society · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Phospho-Form Specific Substrates of Protein Kinase B (AKT1).Frontiers in bioengineering and biotechnology · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. The central role of tRNA in genetic code expansion.Biochimica et biophysica acta. General subjects · 2017
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

5 authors at 1 institution in 1 country.

Michael J HohnDepartment of Molecular Biophysics, Yale University, New Haven, CT 06520-8114, USA.
Hee-Sung Park
Patrick O'Donoghue
Michael Schnitzbauer
Dieter Söll
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

The molecular basis of the genetic code manifests itself in the interaction of the aminoacyl-tRNA synthetases and their cognate tRNAs. The fundamental biological question regarding these enzymes' role in the evolution of the genetic code remains open. Here we probe this question in a system in which the same tRNA species is aminoacylated by two unrelated synthetases. Should this tRNA possess major identity elements common to both enzymes, this would favor a scenario where the aminoacyl-tRNA synthetases evolved in the context of preestablished tRNA identity, i.e., after the universal genetic code emerged. An experimental system is provided by the recently discovered O-phosphoseryl-tRNA synthetase (SepRS), which acylates tRNA(Cys) with phosphoserine (Sep), and the well known cysteinyl-tRNA synthetase, which charges the same tRNA with cysteine. We determined the identity elements of Methanocaldococcus jannaschii tRNA(Cys) in the aminoacylation reaction for the two Methanococcus maripaludis synthetases SepRS (forming Sep-tRNA(Cys)) and cysteinyl-tRNA synthetase (forming Cys-tRNA(Cys)). The major elements, the discriminator base and the three anticodon bases, are shared by both tRNA synthetases. An evolutionary analysis of archaeal, bacterial, and eukaryotic tRNA(Cys) sequences predicted additional SepRS-specific minor identity elements (G37, A47, and A59) and suggested the dominance of vertical inheritance for tRNA(Cys) from a single common ancestor. Transplantation of the identified identity elements into the Escherichia coli tRNA(Gly) scaffold endowed facile phosphoserylation activity on the resulting chimera. Thus, tRNA(Cys) identity is an ancient RNA record that depicts the emergence of the universal genetic code before the evolution of the modern aminoacylation systems.

Indexed as

AminoacylationBase SequenceEscherichia coliEvolution, MolecularGenetic CodeMolecular Sequence DataMutationNucleic Acid ConformationPhylogenyRNA, TransferRNA, Transfer

Identifiers

PMID17110438
PMCPMC1838712
OpenAlexW2150431063

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.