Evidence map›Paper›PMID 27129774›Full record

ArticleThe Journal of biological chemistry2016

PR Domain-containing Protein 7 (PRDM7) Is a Histone 3 Lysine 4 Trimethyltransferase.

Levi L Blazer, Evelyne Lima-Fernandes, Elisa Gibson, Mohammad S Eram, Peter Loppnau, Cheryl H Arrowsmith, Matthieu Schapira, Masoud Vedadi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Pinpointing theFrontiers in genetics · 2021
    Article
  14. Article
  15. Discovery of a chemical probe for PRDM9.Nature communications · 2019
    Article
  16. Article
  17. AberrantGenome research · 2018
    Article
  18. Review
  19. Genes · 2018
    Article
  20. PRDM9 and Its Role in Genetic Recombination.Trends in genetics : TIG · 2018
    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

8 authors at 1 institution in 1 country.

Levi L BlazerFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Evelyne Lima-FernandesFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Elisa GibsonFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Mohammad S EramFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Peter LoppnauFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7.
Cheryl H ArrowsmithFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, the Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, and.
Matthieu SchapiraFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, the Department of Pharmacology and Toxicology, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Masoud VedadiFrom the Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, the Department of Pharmacology and Toxicology, University of Toronto, Toronto, Ontario M5S 1A8, Canada m.vedadi@utoronto.ca.
University of Toronto · CA

Funding

Wellcome Trust
6 · The paper itself

Abstract

PR domain-containing protein 7 (PRDM7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. The two proteins are highly homologous, especially in the catalytic PR/SET domain, where they differ by only three amino acid residues. Here we report that PRDM7 is an efficient methyltransferase that selectively catalyzes the trimethylation of H3 lysine 4 (H3K4) both in vitro and in cells. Through selective mutagenesis we have dissected the functional roles of each of the three divergent residues between the PR domains of PRDM7 and PRDM9. These studies indicate that after a single serine to tyrosine mutation at residue 357 (S357Y), PRDM7 regains the substrate specificities and catalytic activities similar to its evolutionary predecessor, including the ability to efficiently methylate H3K36.

Indexed as

Amino Acid SubstitutionGene DuplicationHEK293 CellsHistone-Lysine N-MethyltransferaseHistonesHumansMethylationMutagenesisMutation, MissenseSubstrate SpecificityHistone-Lysine N-MethyltransferaseHistonesPRDM7 protein, humanPRDM9 protein, humanepigeneticshistone methylationhistone modificationsubstrate specificityzinc finger

Identifiers

PMID27129774
PMCPMC4919437
OpenAlexW2344569636

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.