Evidence map›Paper›PMID 20457752›Full record

ArticleNucleic acids research2010

The archaeal transamidosome for RNA-dependent glutamine biosynthesis.

Theodoros Rampias, Kelly Sheppard, Dieter Söll

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022
    Review
  3. Review
  4. Evolution of the genetic code.Transcription · 2021
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. 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
  11. Emergence and evolution.Topics in current chemistry · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

3 authors at 1 institution in 1 country.

Theodoros RampiasDepartment of Molecular Biophysics and Biochemistry and Department of Chemistry, Yale University, New Haven, CT 06511, USA.
Kelly Sheppard
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 GM022854-34S1
6 · The paper itself

Abstract

Archaea make glutaminyl-tRNA (Gln-tRNA(Gln)) in a two-step process; a non-discriminating glutamyl-tRNA synthetase (ND-GluRS) forms Glu-tRNA(Gln), while the heterodimeric amidotransferase GatDE converts this mischarged tRNA to Gln-tRNA(Gln). Many prokaryotes synthesize asparaginyl-tRNA (Asn-tRNA(Asn)) in a similar manner using a non-discriminating aspartyl-tRNA synthetase (ND-AspRS) and the heterotrimeric amidotransferase GatCAB. The transamidosome, a complex of tRNA synthetase, amidotransferase and tRNA, was first described for the latter system in Thermus thermophilus [Bailly, M., Blaise, M., Lorber, B., Becker, H.D. and Kern, D. (2007) The transamidosome: a dynamic ribonucleoprotein particle dedicated to prokaryotic tRNA-dependent asparagine biosynthesis. Mol. Cell, 28, 228-239.]. Here, we show a similar complex for Gln-tRNA(Gln) formation in Methanothermobacter thermautotrophicus that allows the mischarged Glu-tRNA(Gln) made by the tRNA synthetase to be channeled to the amidotransferase. The association of archaeal ND-GluRS with GatDE (K(D) = 100 ± 22 nM) sequesters the tRNA synthetase for Gln-tRNA(Gln) formation, with GatDE reducing the affinity of ND-GluRS for tRNA(Glu) by at least 13-fold. Unlike the T. thermophilus transamidosome, the archaeal complex does not require tRNA for its formation, is not stable through product (Gln-tRNA(Gln)) formation, and has no major effect on the kinetics of tRNA(Gln) glutamylation nor transamidation. The differences between the two transamidosomes may be a consequence of the fact that ND-GluRS is a class I aminoacyl-tRNA synthetase, while ND-AspRS belongs to the class II family.

Indexed as

Glutamate-tRNA LigaseGlutamineMethanobacteriaceaeNitrogenous Group TransferasesRNA, Transfer, GlnRNA, Transfer, GluTransfer RNA AminoacylationGlutamate-tRNA LigaseGlutamineglutamyl-tRNA(Gln) amidotransferaseNitrogenous Group TransferasesRNA, Transfer, GlnRNA, Transfer, Glu

Identifiers

PMID20457752
PMCPMC2943598
OpenAlexW2068652047

What OpenQuestion holds

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LicenceCC BY-NC
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.