Evidence map›Paper›PMID 22319460›Full record

ArticlePLoS genetics2012

Inter-homolog crossing-over and synapsis in Arabidopsis meiosis are dependent on the chromosome axis protein AtASY3.

Maheen Ferdous, James D Higgins, Kim Osman, Christophe Lambing, Elisabeth Roitinger, Karl Mechtler, Susan J Armstrong, Ruth Perry, Mónica Pradillo, Nieves Cuñado and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
5.9field-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

114 citing papers in PubMed, 186 citations in OpenAlex.

  1. Article
  2. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
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  7. Frontiers in plant science · 2026
    Article
  8. Article
  9. Article
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  11. Article
  12. Meiosis in bulbous flower speciesFrontiers in plant science · 2025
    Article
  13. Article
  14. Heterochromatin in plant meiosis.Nucleus (Austin, Tex.) · 2024
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

54 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 3 countries.

Maheen FerdousSchool of Biosciences, University of Birmingham, United Kingdom.
James D Higgins
Kim Osman
Christophe Lambing
Elisabeth Roitinger
Karl Mechtler
Susan J Armstrong
Ruth Perry
Mónica Pradillo
Nieves Cuñado
F Chris H Franklin
University of Birmingham · GBUniversidad Complutense de Madrid · ESInstitute of Molecular Biotechnology · ATResearch Institute of Molecular Pathology · AT

Funding

Biotechnology and Biological Sciences Research Council BB/E006469/1
6 · The paper itself

Abstract

In this study we have analysed AtASY3, a coiled-coil domain protein that is required for normal meiosis in Arabidopsis. Analysis of an Atasy3-1 mutant reveals that loss of the protein compromises chromosome axis formation and results in reduced numbers of meiotic crossovers (COs). Although the frequency of DNA double-strand breaks (DSBs) appears moderately reduced in Atasy3-1, the main recombination defect is a reduction in the formation of COs. Immunolocalization studies in wild-type meiocytes indicate that the HORMA protein AtASY1, which is related to Hop1 in budding yeast, forms hyper-abundant domains along the chromosomes that are spatially associated with DSBs and early recombination pathway proteins. Loss of AtASY3 disrupts the axial organization of AtASY1. Furthermore we show that the AtASY3 and AtASY1 homologs BoASY3 and BoASY1, from the closely related species Brassica oleracea, are co-immunoprecipitated from meiocyte extracts and that AtASY3 interacts with AtASY1 via residues in its predicted coiled-coil domain. Together our results suggest that AtASY3 is a functional homolog of Red1. Since studies in budding yeast indicate that Red1 and Hop1 play a key role in establishing a bias to favor inter-homolog recombination (IHR), we propose that AtASY3 and AtASY1 may have a similar role in Arabidopsis. Loss of AtASY3 also disrupts synaptonemal complex (SC) formation. In Atasy3-1 the transverse filament protein AtZYP1 forms small patches rather than a continuous SC. The few AtMLH1 foci that remain in Atasy3-1 are found in association with the AtZYP1 patches. This is sufficient to prevent the ectopic recombination observed in the absence of AtZYP1, thus emphasizing that in addition to its structural role the protein is important for CO formation.

Indexed as

Chromosome PairingCrossing Over, GeneticArabidopsisArabidopsis ProteinsBrassicaChromosomes, PlantDNA-Binding ProteinsDNA Breaks, Double-StrandedMeiosisMutationRecombination, GeneticSaccharomyces cerevisiae ProteinsSynaptonemal ComplexArabidopsis ProteinsASY1 protein, ArabidopsisASY3 protein, ArabidopsisDNA-Binding ProteinsHOP1 protein, S cerevisiaeRED1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22319460
PMCPMC3271061
OpenAlexW2071996109

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.