Evidence map›Paper›PMID 22391451›Full record

ArticleGenes & development2012

Beyond tRNA cleavage: novel essential function for yeast tRNA splicing endonuclease unrelated to tRNA processing.

Nripesh Dhungel, Anita K Hopper

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. The highly conserved intron of tyrosine tRNA is critical forProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Comparative parallel analysis of RNA ends identifies mRNA substrates of a tRNA splicing endonuclease-initiated mRNA decay pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Metabolic influences on RNA biology and translation.Critical reviews in biochemistry and molecular biology · 2017
    Review
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Nripesh DhungelDepartment of Molecular Genetics, Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Anita K Hopper
The 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
NIGMS NIH HHS GM27930NIGMS NIH HHS R01 GM027930
6 · The paper itself

Abstract

Pre-tRNA splicing is an essential process in all eukaryotes. In yeast and vertebrates, the enzyme catalyzing intron removal from pre-tRNA is a heterotetrameric complex (splicing endonuclease [SEN] complex). Although the SEN complex is conserved, the subcellular location where pre-tRNA splicing occurs is not. In yeast, the SEN complex is located at the cytoplasmic surface of mitochondria, whereas in vertebrates, pre-tRNA splicing is nuclear. We engineered yeast to mimic the vertebrate cell biology and demonstrate that all three steps of pre-tRNA splicing, as well as tRNA nuclear export and aminoacylation, occur efficiently when the SEN complex is nuclear. However, nuclear pre-tRNA splicing fails to complement growth defects of cells with defective mitochondrial-located splicing, suggesting that the yeast SEN complex surprisingly serves a novel and essential function in the cytoplasm that is unrelated to tRNA splicing. The novel function requires all four SEN complex subunits and the catalytic core. A subset of pre-rRNAs accumulates when the SEN complex is restricted to the nucleus, indicating that the SEN complex moonlights in rRNA processing. Thus, findings suggest that selection for the subcellular distribution of the SEN complex may reside not in its canonical, but rather in a novel, activity.

Indexed as

AminoacylationCell NucleusCytoplasmEndoribonucleasesRNA, TransferSaccharomyces cerevisiaeEndoribonucleasesRNA, Transfersplicing endonuclease

Identifiers

PMID22391451
PMCPMC3305987
OpenAlexW2121919944

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.