The Nematostella synaptonemal complex mediates divergent and sex-specific meiotic programs

preprint OA: closed
Full text JSON View at publisher

Abstract

Throughout eukaryotes, the synaptonemal complex (SC) is a supramolecular structure essential for meiotic chromosome dynamics and sexual reproduction. While metazoan SC proteins display significant sequence divergence, the lack of functional analyses beyond bilaterian models has obscured a mechanistic understanding of SC evolution. Here we report that the sea anemone Nematostella vectensis exhibits synapsis of homologous chromosomes in a classic zipper-like manner and expresses eight orthologs of ten known vertebrate SC proteins. Surprisingly, mutagenesis of the core SC components sycp1, syce2 , and sycp3 resulted in divergent and sexually dimorphic phenotypes, indicating the functional diversification of these conserved factors. Combined, these findings challenge the assumption that the conservation of protein sequence or ultrastructure implies mechanistic homology.
Full text 964 characters · extracted from oa-doi-fallback · click to expand
Abstract Throughout eukaryotes, the synaptonemal complex (SC) is a supramolecular structure essential for meiotic chromosome dynamics and sexual reproduction. While metazoan SC proteins display significant sequence divergence, the lack of functional analyses beyond bilaterian models has obscured a mechanistic understanding of SC evolution. Here we report that the sea anemone Nematostella vectensis exhibits synapsis of homologous chromosomes in a classic zipper-like manner and expresses eight orthologs of ten known vertebrate SC proteins. Surprisingly, mutagenesis of the core SC components sycp1, syce2, and sycp3 resulted in divergent and sexually dimorphic phenotypes, indicating the functional diversification of these conserved factors. Combined, these findings challenge the assumption that the conservation of protein sequence or ultrastructure implies mechanistic homology. Competing Interest Statement The authors have declared no competing interest.

Text is read by the "Ask this paper" AI Q&A widget below. Extraction quality varies by source — PMC NXML preserves structure cleanly, OA-HTML may include some navigation residue, and OA-PDF can have broken hyphenation. The publisher copy (via DOI) is the canonical version.

My notes (saved in your browser only)

Ask this paper AI returns verbatim quotes from the full text · source: oa-doi-fallback

Answers must be backed by verbatim quotes from this paper's full text. Hallucinated quotes are dropped automatically; if no verbatim passage answers the question, we say so. How this works

Citation neighborhood (no data yet)

We don't have any in-corpus citations linked to this paper yet. This is a recent paper (2026) — citers typically take a year or two to land, and the OpenAlex reference graph may still be filling in.

Source provenance

europepmc
last seen: 2026-05-20T01:45:00.602351+00:00