Evidence map›Paper›PMID 21307182›Full record

ArticleRNA (New York, N.Y.)2011

A role for tRNA(His) guanylyltransferase (Thg1)-like proteins from Dictyostelium discoideum in mitochondrial 5'-tRNA editing.

Maria G Abad, Yicheng Long, Allison Willcox, Jonatha M Gott, Michael W Gray, Jane E Jackman

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. A comparison ofbioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. From end to end: tRNA editing at 5'- and 3'-terminal positions.International journal of molecular sciences · 2014
    Review
  20. 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

6 authors at 3 institutions in 2 countries.

Maria G AbadDepartment of Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Yicheng Long
Allison Willcox
Jonatha M Gott
Michael W Gray
Jane E Jackman
The Ohio State University · USCase Western Reserve University · USDalhousie University · CA

Funding

Molecular Mechanism and Biological Function of 3'-5' PolymerasesR01GM087543 · NIGMS · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH · 2010 to 2019
$2.7M
TRANSCRIPTION AND INSERTIONAL RNA EDITING IN PHYSARUMR01GM054663 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI GOTT, JONATHA MARY · 1998 to 2006
$2.2M
TRANSCRIPTION AND INSERTIONAL RNA EDITING IN PHYSARUMR55GM054663 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI GOTT, JONATHA MARY · 1996 to 1996
–
NIGMS NIH HHS GM054663NIGMS NIH HHS GM087543NIGMS NIH HHS R01 GM054663NIGMS NIH HHS R01 GM087543
6 · The paper itself

Abstract

Genes with sequence similarity to the yeast tRNA(His) guanylyltransferase (Thg1) gene have been identified in all three domains of life, and Thg1 family enzymes are implicated in diverse processes, ranging from tRNA(His) maturation to 5'-end repair of tRNAs. All of these activities take advantage of the ability of Thg1 family enzymes to catalyze 3'-5' nucleotide addition reactions. Although many Thg1-containing organisms have a single Thg1-related gene, certain eukaryotic microbes possess multiple genes with sequence similarity to Thg1. Here we investigate the activities of four Thg1-like proteins (TLPs) encoded by the genome of the slime mold, Dictyostelium discoideum (a member of the eukaryotic supergroup Amoebozoa). We show that one of the four TLPs is a bona fide Thg1 ortholog, a cytoplasmic G(-1) addition enzyme likely to be responsible for tRNA(His) maturation in D. discoideum. Two other D. discoideum TLPs exhibit biochemical activities consistent with a role for these enzymes in mitochondrial 5'-tRNA editing, based on their ability to efficiently repair the 5' ends of mitochondrial tRNA editing substrates. Although 5'-tRNA editing was discovered nearly two decades ago, the identity of the protein(s) that catalyze this activity has remained elusive. This article provides the first identification of any purified protein that appears to play a role in the 5'-tRNA editing reaction. Moreover, the presence of multiple Thg1 family members in D. discoideum suggests that gene duplication and divergence during evolution has resulted in paralogous proteins that use 3'-5' nucleotide addition reactions for diverse biological functions in the same organism.

Indexed as

RNA EditingAmino Acid SequenceCatalysisDictyosteliumMolecular Sequence DataNucleotidyltransferasesRNA, Transfer, Amino AcylSequence AlignmentNucleotidyltransferasesRNA, Transfer, Amino AcyltRNA guanylyltransferase

Identifiers

PMID21307182
PMCPMC3062173
OpenAlexW2131795917

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.