Evidence map›Paper›PMID 15917221›Full record

ArticleThe Journal of biological chemistry2005

Association between Archaeal prolyl- and leucyl-tRNA synthetases enhances tRNA(Pro) aminoacylation.

Mette Praetorius-Ibba, Theresa E Rogers, Rachel Samson, Zvi Kelman, Michael Ibba

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A self-referential model for the formation of the genetic code.Theory in biosciences = Theorie in den Biowissenschaften · 2008
    Article
  8. Review
  9. Article
  10. Article
  11. tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNA
    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

5 authors at 2 institutions in 1 country.

Mette Praetorius-IbbaDepartment of Microbiology, The Ohio State University, Columbus, Ohio 43210-1292, USA. ibba.1@osu.edu
Theresa E Rogers
Rachel Samson
Zvi Kelman
Michael Ibba
The Ohio State University · USBiotechnology Institute · US

Funding

Mechanisms of translational controlR01GM065183 · NIGMS · OHIO STATE UNIVERSITY · PI DUNHAM, CHRISTINE M, FREDRICK, KURT L · 2003 to 2020
$4.9M
NIGMS NIH HHS GM 65183NIGMS NIH HHS R01 GM065183
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetase-containing complexes have been identified in different eukaryotes, and their existence has also been suggested in some Archaea. To investigate interactions involving aminoacyl-tRNA synthetases in Archaea, we undertook a yeast two-hybrid screen for interactions between Methanothermobacter thermautotrophicus proteins using prolyl-tRNA synthetase (ProRS) as the bait. Interacting proteins identified included components of methanogenesis, protein-modifying factors, and leucyl-tRNA synthetase (LeuRS). The association of ProRS with LeuRS was confirmed in vitro by native gel electrophoresis and size exclusion chromatography. Determination of the steady-state kinetics of tRNA(Pro) charging showed that the catalytic efficiency (k(cat)/K(m)) of ProRS increased 5-fold in the complex with LeuRS compared with the free enzyme, whereas the K(m) for proline was unchanged. No significant changes in the steady-state kinetics of LeuRS aminoacylation were observed upon the addition of ProRS. These findings indicate that ProRS and LeuRS associate in M. thermautotrophicus and suggest that this interaction contributes to translational fidelity by enhancing tRNA aminoacylation by ProRS.

Indexed as

Amino Acyl-tRNA SynthetasesChromatographyChromatography, GelDNA, ComplementaryElectrophoresis, Polyacrylamide GelEscherichia coliGene LibraryHistidineKineticsLeucine-tRNA LigaseMethanobacteriaceaePhenotypeProtein BindingProtein BiosynthesisRNA, MessengerRNA, Transfer, ProAmino Acyl-tRNA SynthetasesDNA, ComplementaryHistidineLeucine-tRNA Ligaseprolyl T RNA synthetaseRNA, MessengerRNA, Transfer, Pro

Identifiers

PMID15917221
PMCPMC1242193
OpenAlexW1970946409

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.