Evidence map›Paper›PMID 36942481›Full record

ArticleNucleic acids research2023

Biochemical characterisation of Mer3 helicase interactions and the protection of meiotic recombination intermediates.

Veronika Altmannova, Magdalena Firlej, Franziska Müller, Petra Janning, Rahel Rauleder, Dorota Rousova, Andreas Schäffler, Tanja Bange, John R Weir

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024
    Review
  10. 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

9 authors at 3 institutions in 1 country.

Veronika AltmannovaFriedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, 72076 Tübingen, Germany.
Magdalena FirlejFriedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, 72076 Tübingen, Germany.
Franziska MüllerDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0002-4880-9269
Petra JanningDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.
Rahel RaulederFriedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, 72076 Tübingen, Germany.
Dorota RousovaFriedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, 72076 Tübingen, Germany.
Andreas SchäfflerFriedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, 72076 Tübingen, Germany.
Tanja BangeInstitute of Medical Psychology, Faculty of Medicine, LMU Munich, Germany.
John R WeirFriedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, 72076 Tübingen, Germany.ORCID 0000-0002-6904-0284
Max Planck Society · DEMax Planck Institute of Molecular Physiology · DELudwig-Maximilians-Universität München · DE

Funding

Wellcome Trust
6 · The paper itself

Abstract

Crossing over between homologs is critical for the stable segregation of chromosomes during the first meiotic division. Saccharomyces cerevisiae Mer3 (HFM1 in mammals) is a SF2 helicase and member of the ZMM group of proteins, that facilitates the formation of the majority of crossovers during meiosis. Here, we describe the structural organisation of Mer3 and using AlphaFold modelling and XL-MS we further characterise the previously described interaction with Mlh1-Mlh2. We find that Mer3 also forms a previously undescribed complex with the recombination regulating factors Top3 and Rmi1 and that this interaction is competitive with Sgs1BLM helicase. Using in vitro reconstituted D-loop assays we show that Mer3 inhibits the anti-recombination activity of Sgs1 helicase, but only in the presence of Dmc1. Thus we provide a mechanism whereby Mer3 interacts with a network of proteins to protect Dmc1 derived D-loops from dissolution.

Indexed as

DNA HelicasesHomologous RecombinationMeiosisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBinding, CompetitiveCell Cycle ProteinsCrossing Over, GeneticDNA-Binding ProteinsMutL Protein Homolog 1MutL ProteinsProtein BindingProtein FoldingRecQ HelicasesCell Cycle ProteinsDMC1 protein, S cerevisiaeDNA-Binding ProteinsDNA HelicasesHFM1 protein, S cerevisiaeMLH1 protein, S cerevisiaeMLH2 protein, S cerevisiaeMutL Protein Homolog 1MutL ProteinsRecQ HelicasesRmi1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiaeTOP3 protein, S cerevisiae

Identifiers

PMID36942481
PMCPMC10201424
OpenAlexW4328049435

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.