Dynamic molecular architecture of the synaptonemal complex

During meiosis, pairing between homologous chromosomes is stabilized by the assembly of the synaptonemal complex (SC). The SC ensures the formation of crossovers between homologous chromosomes and regulates their distribution. However, how the SC regulates crossover formation remains elusive. We isolated an unusual mutation in <i>Caenorhabditis elegans</i> that disrupts crossover interference but not SC assembly. This mutation alters the unique C terminal domain of an essential SC protein, SYP-4, a likely ortholog of the vertebrate SC protein SIX6OS1. We use three-dimensional stochastic optical reconstruction microscopy (3D-STORM) to interrogate the molecular architecture of the SC from wild-type and mutant <i>C. elegans</i> animals. Using a probabilistic mapping approach to analyze super-resolution image data, we detect changes in the organization of the synaptonemal complex in wild-type animals that coincide with crossover designation. We also found that our <i>syp-4</i> mutant perturbs SC architecture. Our findings add to growing evidence that the SC is an active material whose molecular organization contributes to chromosome-wide crossover regulation.

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Publication Details

Journal
Science Advances
Published
2025-01-22
DOI
https://doi.org/10.1126/sciadv.adq9374
Citations
12
Primary Topic
DNA Repair Mechanisms
Type
article
Field-Weighted Citation Impact
9.67
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article

Dynamic molecular architecture of the synaptonemal complex

Abby F. Dernburg, Simone Köhler, Michal Wojcik, Ke Xu
12 citations
Science Advances
DNA Repair Mechanisms
9.67
article

Dynamic molecular architecture of the synaptonemal complex

Abby F. Dernburg, Simone Köhler, Michal Wojcik, Ke Xu
article en
12 citations

Abstract

During meiosis, pairing between homologous chromosomes is stabilized by the assembly of the synaptonemal complex (SC). The SC ensures the formation of crossovers between homologous chromosomes and regulates their distribution. However, how the SC regulates crossover formation remains elusive. We isolated an unusual mutation in <i>Caenorhabditis elegans</i> that disrupts crossover interference but not SC assembly. This mutation alters the unique C terminal domain of an essential SC protein, SYP-4, a likely ortholog of the vertebrate SC protein SIX6OS1. We use three-dimensional stochastic optical reconstruction microscopy (3D-STORM) to interrogate the molecular architecture of the SC from wild-type and mutant <i>C. elegans</i> animals. Using a probabilistic mapping approach to analyze super-resolution image data, we detect changes in the organization of the synaptonemal complex in wild-type animals that coincide with crossover designation. We also found that our <i>syp-4</i> mutant perturbs SC architecture. Our findings add to growing evidence that the SC is an active material whose molecular organization contributes to chromosome-wide crossover regulation.

Science AdvancesVol. 11(4)
QB3 (US), Howard Hughes Medical Institute (US), Lawrence Berkeley National Laboratory (US), Chan Zuckerberg Initiative (United States) (US), University of California, Berkeley (US)
Openalex Percentile: Top 2%
DNA Repair Mechanisms
9.67
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Dynamic molecular architecture of the synaptonemal complex — Abby F. Dernburg, Simone Köhler, et al. · Science Advances (2025) | TGRS Research Map | TGRS