Evidence map›Paper›PMID 12775689›Full record

ArticleJournal of bacteriology2003

Protein synthesis in Escherichia coli with mischarged tRNA.

Bokkee Min, Makoto Kitabatake, Carla Polycarpo, Joanne Pelaschier, Gregory Raczniak, Benfang Ruan, Hiroyuki Kobayashi, Suk Namgoong, Dieter Söll

Abstract read
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Impact of queuosine modification of endogenousFrontiers in molecular biosciences · 2022
    Article
  3. Article
  4. Review
  5. tRNA acceptor stem and anticodon bases form independent codes related to protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Article
  7. Article
  8. Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  9. Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Quality control despite mistranslation caused by an ambiguous genetic code.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  11. Article
  12. Amino acid modifications on tRNA.Acta biochimica et biophysica Sinica · 2008
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. 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

9 authors.

Bokkee MinDepartment of Molecular Biophysics, Yale University, New Haven, Connecticut 06520-8114, USA.
Makoto Kitabatake
Carla Polycarpo
Joanne Pelaschier
Gregory Raczniak
Benfang Ruan
Hiroyuki Kobayashi
Suk Namgoong
Dieter Söll

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two types of aspartyl-tRNA synthetase exist: the discriminating enzyme (D-AspRS) forms only Asp-tRNA(Asp), while the nondiscriminating one (ND-AspRS) also synthesizes Asp-tRNA(Asn), a required intermediate in protein synthesis in many organisms (but not in Escherichia coli). On the basis of the E. coli trpA34 missense mutant transformed with heterologous ND-aspS genes, we developed a system with which to measure the in vivo formation of Asp-tRNA(Asn) and its acceptance by elongation factor EF-Tu. While large amounts of Asp-tRNA(Asn) are detrimental to E. coli, smaller amounts support protein synthesis and allow the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase.

Indexed as

Aspartate-tRNA LigaseEscherichia coliEscherichia coli ProteinsMutation, MissensePeptide Elongation FactorsRNA, BacterialRNA, TransferRNA, Transfer, Amino AcylTransformation, BacterialTryptophanTryptophan Synthaseasparaginyl-tRNA synthetaseAspartate-tRNA LigaseEscherichia coli ProteinsPeptide Elongation FactorsRNA, BacterialRNA, TransferRNA, Transfer, Amino AcylTryptophanTryptophan Synthase

Identifiers

PMID12775689
PMCPMC156233

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.