Evidence map›Paper›PMID 25261850›Full record

ReviewGene2015

The cytoplasmic and nuclear populations of the eukaryote tRNA-isopentenyl transferase have distinct functions with implications in human cancer.

P J Smaldino, D F Read, M Pratt-Hyatt, A K Hopper, D R Engelke

Open access · greenAbstract readReview
In one paragraph

Review in Gene, 2015. 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
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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Failure to Guard: Mitochondrial Protein Quality Control in Cancer.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity.Journal of visualized experiments : JoVE · 2018
    Article
  10. Article
  11. Review
  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

5 authors at 3 institutions in 1 country.

P J SmaldinoDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: smaldino@med.umich.edu.
D F ReadDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
M Pratt-HyattDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; The Great Plains Laboratory, 11813W. 77th St. Lenexa KS 66214, USA.
A K HopperDepartment of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
D R EngelkeDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: engelke@med.umich.edu.
University of Michigan–Ann Arbor · USNorthern Great Plains Research Laboratory · USThe Ohio State University · US

Funding

YEAST GENES IN RNA PROCESSING &NUCLEUS/CYTOSOL EXCHANGER01GM027930 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI HOPPER, ANITA K · 1985 to 2014
$4.6M
Transcriptional Silencing Near tRNA GenesR01GM063142 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ENGELKE, DAVID R · 2001 to 2004
$1.2M
NIGMS NIH HHS GM27930NIGMS NIH HHS R01 GM027930NIGMS NIH HHS R01 GM063142
6 · The paper itself

Abstract

Mod5 is the yeast tRNA isopentenyl transferase, an enzyme that is conserved from bacteria to humans. Mod5 is primarily cytoplasmic where it modifies the A37 position of a few tRNAs, and the yeast enzyme has been shown capable of forming heritable, amyloid-like aggregates that confer a selective advantage in the presence of specific antifungal agents. A subpopulation of Mod5 is also found associated with nuclear tRNA genes, where it contributes tRNA-gene mediated (tgm) silencing of local transcription by RNA polymerase II. The tgm-silencing function of Mod5 has been observed in yeast and a Mod5-deletion in yeast can be complemented by the plant and human tRNA isopentenyl transferases, but not the bacterial enzymes, possibly due to the lack of an extended C-terminal domain found in eukaryotes. In light of this additional nuclear role for Mod5 we discuss the proposed role of the human homologue of Mod5, TRIT1, as a tumor suppressor protein.

Indexed as

Alkyl and Aryl TransferasesAmino Acid SequenceCell NucleusCytoplasmGenes, Tumor SuppressorHumansMolecular Sequence DataNeoplasmsProtein FoldingSequence Homology, Amino AcidAlkyl and Aryl TransferasesTRIT1 protein, humanMod5PrionTRIT1tRNAtRNA gene-mediated silencingtRNA modificationTumor suppressor

Identifiers

PMID25261850
PMCPMC4272631
OpenAlexW2025674041

What OpenQuestion holds

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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.