Evidence map›Paper›PMID 28527011›Full record

ArticleChromosoma2017

The PRDM9 KRAB domain is required for meiosis and involved in protein interactions.

Yukiko Imai, Frédéric Baudat, Miguel Taillepierre, Marcello Stanzione, Attila Toth, Bernard de Massy

Open access · hybridAbstract read
In one paragraph

Article in Chromosoma, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 85 citations in OpenAlex.

  1. Controlling Meiotic Double-Strand Break Formation in Mice: A Web of Multivalent Protein-Protein Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. On the origin of PRDM9-guided recombination hotspots.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  12. Article
  13. Genetic control of meiosis surveillance mechanisms in mammals.Frontiers in cell and developmental biology · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Chromosome architecture and homologous recombination in meiosis.Frontiers in cell and developmental biology · 2022
    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 2 institutions in 2 countries.

Yukiko ImaiInstitut de Génétique Humaine UMR9002 CNRS-Université de Montpellier, 141 rue de la cardonille, 34396, Montpellier cedex 05, France.
Frédéric BaudatInstitut de Génétique Humaine UMR9002 CNRS-Université de Montpellier, 141 rue de la cardonille, 34396, Montpellier cedex 05, France.
Miguel TaillepierreSEAT-TAAM CNRS Phenomin UPS44, 7 rue Guy Môquet, 94800, Villejuif, France.
Marcello StanzioneFaculty of Medicine at the TU Dresden, Institute of Physiological Chemistry, Fetscherstraße 74, 01307, Dresden, Germany.
Attila TothFaculty of Medicine at the TU Dresden, Institute of Physiological Chemistry, Fetscherstraße 74, 01307, Dresden, Germany.
Bernard de MassyInstitut de Génétique Humaine UMR9002 CNRS-Université de Montpellier, 141 rue de la cardonille, 34396, Montpellier cedex 05, France. bernard.de-massy@igh.cnrs.fr.ORCID http://orcid.org/0000-0002-0950-2758
Centre National de la Recherche Scientifique · FRTechnische Universität Dresden · DE

Funding

DFG SPP1384:TO421/4-2DFG TO421/3-2DFG TO421/5-1DFG TO421/6-1DFG TO421/8-1DFG TO421/8-2European Research Council 322788
6 · The paper itself

Abstract

PR domain-containing protein 9 (PRDM9) is a major regulator of the localization of meiotic recombination hotspots in the human and mouse genomes. This role involves its DNA-binding domain, which is composed of a tandem array of zinc fingers, and PRDM9-dependent trimethylation of histone H3 at lysine 4. PRDM9 is a member of the PRDM family of transcription regulators, but unlike other family members, it contains a Krüppel-associated box (KRAB)-related domain that is predicted to be a potential protein interaction domain. Here, we show that truncation of the KRAB domain of mouse PRDM9 leads to loss of PRDM9 function and altered meiotic prophase and gametogenesis. In addition, we identified proteins that interact with the KRAB domain of PRDM9 in yeast two-hybrid assay screens, particularly CXXC1, a member of the COMPASS complex. We also show that CXXC1 interacts with IHO1, an essential component of the meiotic double-strand break (DSB) machinery. As CXXC1 is orthologous to Saccharomyces cerevisiae Spp1 that links DSB sites to the DSB machinery on the chromosome axis, we propose that these molecular interactions involved in the regulation of meiotic DSB formation are conserved in mouse meiosis.

Indexed as

Protein Interaction Domains and MotifsAnimalsFemaleGonadsHistone-Lysine N-MethyltransferaseImmunohistochemistryMaleMeiosisMiceMice, KnockoutModels, BiologicalProtein BindingSaccharomyces cerevisiaeTrans-ActivatorsCxxc1 protein, mouseHistone-Lysine N-Methyltransferaseprdm9 protein, mouseTrans-ActivatorsCXXC1IHO1MeiosisPRDM9 KRAB domainProtein interactionsRecombination

Identifiers

PMID28527011
PMCPMC5688218
OpenAlexW2615019156

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.