Evidence map›Paper›PMID 23241387›Full record

ArticleNucleic acids research2013

Absence of a universal element for tRNAHis identity in Acanthamoeba castellanii.

Bhalchandra S Rao, Fuad Mohammad, Michael W Gray, Jane E Jackman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. 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
0.7field-weighted citation impact, top 30% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. A comparison ofbioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Article
  4. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. A Temporal Order in 5'- and 3'- Processing of Eukaryotic tRNAInternational journal of molecular sciences · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. From end to end: tRNA editing at 5'- and 3'-terminal positions.International journal of molecular sciences · 2014
    Review
  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

4 authors at 2 institutions in 2 countries.

Bhalchandra S RaoDepartment of Chemistry and Biochemistry and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Fuad Mohammad
Michael W Gray
Jane E Jackman
Dalhousie University · CAThe Ohio State University · US

Funding

Molecular Mechanism and Biological Function of 3'-5' PolymerasesR01GM087543 · NIGMS · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH · 2010 to 2019
$2.7M
NIGMS NIH HHS GM087543NIGMS NIH HHS R01 GM087543
6 · The paper itself

Abstract

The additional G(-1) nucleotide on tRNA(His) is a nearly universal feature that specifies tRNA(His) identity in all three domains of life. In eukaryotes, the G(-1) identity element is obtained by a post-transcriptional pathway, through the unusual 3'-5' polymerase activity of the highly conserved tRNA(His) guanylyltransferase (Thg1) enzyme, and no examples of eukaryotic histidyl-tRNAs that lack this essential element have been identified. Here we report that the eukaryote Acanthamoeba castellanii lacks the G(-1) identity element on its tRNA(His), consistent with the lack of a gene encoding a bona fide Thg1 ortholog in the A. castellanii genome. Moreover, the cytosolic histidyl-tRNA synthetase in A. castellanii exhibits an unusual tRNA substrate specificity, efficiently aminoacylating tRNA(His) regardless of the presence of G(-1). A. castellanii does contain two Thg1-related genes (encoding Thg1-like proteins, TLPs), but the biochemical properties we associate here with these proteins are consistent with a function for these TLPs in separate pathways unrelated to tRNA(His) metabolism, such as mitochondrial tRNA repair during 5'-editing.

Indexed as

Acanthamoeba castellaniiDNA-Directed RNA PolymerasesHistidine-tRNA LigaseNucleotidyltransferasesRNARNA EditingRNA, MitochondrialRNA, TransferRNA, Transfer, HisDNA-Directed RNA PolymerasesHistidine-tRNA LigaseNucleotidyltransferasesRNARNA, MitochondrialRNA, TransferRNA, Transfer, HistRNA guanylyltransferase

Identifiers

PMID23241387
PMCPMC3561963
OpenAlexW2171795326

What OpenQuestion holds

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LicenceCC BY-NC
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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.