Evidence map›Paper›PMID 20053728›Full record

ArticleNucleic acids research2010

Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p.

Chi-Ming Wong, Hei-Man Vincent Tang, Ka-Yiu Edwin Kong, Gee-Wan Oscar Wong, Hongfang Qiu, Dong-Yan Jin, Alan G Hinnebusch

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Citrullination and the protein code: crosstalk between post-translational modifications in cancer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  3. Article
  4. Article
  5. Protein arginine methylation in transcription and epigenetic regulation.Frontiers in epigenetics and epigenomics · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Keeping mRNPs in check during assembly and nuclear export.Nature reviews. Molecular cell biology · 2011
    Article
  19. The Role of Protein Arginine Methylation in mRNP Dynamics.Molecular biology international · 2011
    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

7 authors at 3 institutions in 2 countries.

Chi-Ming WongDepartment of Biochemistry, The University of Hong Kong, Hong Kong. wispwong@hkucc.hku.hk
Hei-Man Vincent Tang
Ka-Yiu Edwin Kong
Gee-Wan Oscar Wong
Hongfang Qiu
Dong-Yan Jin
Alan G Hinnebusch
National Institutes of Health · USUniversity of Hong Kong · HKEunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Transcriptional Regulation of Gene ExpressionZIAHD008899 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HINNEBUSCH, ALAN G · 2010 to 2025
$11.6M
Intramural NIH HHS
6 · The paper itself

Abstract

The heterogeneous nuclear ribonucleoprotein Npl3p of budding yeast is a substrate of arginine methyltransferase Hmt1p, but the role of Hmt1p in regulating Npl3p's functions in transcription antitermination and elongation were unknown. We found that mutants lacking Hmt1p methyltransferase activity exhibit reduced recruitment of Npl3p, but elevated recruitment of a component of mRNA cleavage/termination factor CFI, to the activated GAL10-GAL7 locus. Consistent with this, hmt1 mutants displayed increased termination at the defective gal10-Delta56 terminator. Remarkably, hmt1Delta cells also exhibit diminished recruitment of elongation factor Tho2p and a reduced rate of transcription elongation in vivo. Importantly, the defects in Npl3p and Tho2p recruitment, antitermination and elongation in hmt1Delta cells all were mitigated by substitutions in Npl3p RGG repeats that functionally mimic arginine methylation by Hmt1p. Thus, Hmt1p promotes elongation and suppresses termination at cryptic terminators by methylating RGG repeats in Npl3p. As Hmt1p stimulates dissociation of Tho2p from an Npl3p-mRNP complex, it could act to recycle these elongation and antitermination factors back to sites of ongoing transcription.

Indexed as

Gene Expression RegulationTranscription, GeneticGene DeletionMethylationmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsProtein-Arginine N-MethyltransferasesRepetitive Sequences, Amino AcidRepressor ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsGAL10 protein, S cerevisiaeHMT1 protein, S cerevisiaeHRP1 protein, S cerevisiaemRNA Cleavage and Polyadenylation FactorsNPL3 protein, S cerevisiaeNuclear ProteinsProtein-Arginine N-MethyltransferasesRepressor ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTHO2 protein, S cerevisiaeTrans-ActivatorsTranscription Factors

Identifiers

PMID20053728
PMCPMC2853106
OpenAlexW2120341208

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.