Evidence map›Paper›PMID 16065067›Full record

ArticleEMBO reports2005

Stationary-phase expression and aminoacylation of a transfer-RNA-like small RNA.

Sandro F Ataide, Brian C Jester, Kevin M Devine, Michael Ibba

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Emergence and evolution.Topics in current chemistry · 2014
    Review
  4. Article
  5. Analysis of aminoacyl- and peptidyl-tRNAs by gel electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2012
    Article
  6. Article
  7. Review
  8. Review
  9. RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  10. Article
  11. Article
  12. Article
  13. 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

4 authors at 2 institutions in 2 countries.

Sandro F AtaideDepartment of Microbiology, The Ohio State University, Columbus, 43210-1292, USA.
Brian C Jester
Kevin M Devine
Michael Ibba
The Ohio State University · USTrinity College Dublin · IE

Funding

Mechanisms of translational controlR01GM065183 · NIGMS · OHIO STATE UNIVERSITY · PI DUNHAM, CHRISTINE M, FREDRICK, KURT L · 2003 to 2020
$4.9M
NIGMS NIH HHS GM65183NIGMS NIH HHS R01 GM065183
6 · The paper itself

Abstract

Genome-scale analyses have shown numerous functional duplications in the canonical translational machinery. One of the most striking examples is the occurrence of unrelated class I and class II lysyl-transfer RNA synthetases (LysRS), which together may aminoacylate non-canonical tRNAs. We show that, in Bacillus cereus, the two LysRSs together aminoacylate a small RNA of unknown function named tRNA(Other), and that the aminoacylated product stably binds translation elongation factor Tu. In vitro reconstitution of a defined lysylation system showed that Lys-tRNA(Other) is synthesized in the presence of both LysRSs, but not by either alone. In vivo analyses showed that the class 2 LysRS was present both during and after exponential growth, whereas the class I enzyme and tRNA(Other) were predominantly produced during the stationary phase. Aminoacylation of tRNA(Other) was also found to be confined to the stationary phase, which suggests a role for this non-canonical tRNA in growth-phase-specific protein synthesis.

Indexed as

AminoacylationAmino Acyl-tRNA SynthetasesBacillus cereusBacillus subtilisBacterial Physiological PhenomenaChromatographyElectrophoresis, Polyacrylamide GelGenomeGenome, BacterialImmunoblottingLysinePeptide Elongation Factor TuProtein Structure, SecondaryReverse Transcriptase Polymerase Chain ReactionRNARNA, TransferAmino Acyl-tRNA SynthetasesLysinePeptide Elongation Factor TuRNARNA, Transfer

Identifiers

PMID16065067
PMCPMC1369145
OpenAlexW2097336880

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.