ArticleNature communications2023
Ubiquitination-mediated Golgi-to-endosome sorting determines the toxin-antidote duality of fission yeast wtf meiotic drivers.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Recombination shapes the diversification of theeLife · 2026Article
- The evolutionary genomics of meiotic drive.Molecular biology and evolution · 2026Article
- Comparative ubiquitinome analysis reveals the roles of protein ubiquitination in the heat stress response fromApplied and environmental microbiology · 2025Article
- Recurrent evolution of selfishness from an essential tRNA synthetase in Caenorhabditis tropicalis.Nature ecology & evolution · 2025Article
- Functional constraints of wtf killer meiotic drivers.PLoS genetics · 2025Article
- Functional constraints ofbioRxiv : the preprint server for biology · 2025Article
- A meiotic driver hijacks an epigenetic reader to disrupt mitosis in noncarrier offspring.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural duality enables a single protein to act as a toxin-antidote pair for meiotic drive.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Evolutionary Modes of wtf Meiotic Driver Genes in Schizosaccharomyces pombe.Genome biology and evolution · 2024Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Killer meiotic drivers (KMDs) skew allele transmission in their favor by killing meiotic progeny not inheriting the driver allele. Despite their widespread presence in eukaryotes, the molecular mechanisms behind their selfish behavior are poorly understood. In several fission yeast species, single-gene KMDs belonging to the wtf gene family exert selfish killing by expressing a toxin and an antidote through alternative transcription initiation. Here we investigate how the toxin and antidote products of a wtf-family KMD gene can act antagonistically. Both the toxin and the antidote are multi-transmembrane proteins, differing only in their N-terminal cytosolic tails. We find that the antidote employs PY motifs (Leu/Pro-Pro-X-Tyr) in its N-terminal cytosolic tail to bind Rsp5/NEDD4 family ubiquitin ligases, which ubiquitinate the antidote. Mutating PY motifs or attaching a deubiquitinating enzyme transforms the antidote into a toxic protein. Ubiquitination promotes the transport of the antidote from the trans-Golgi network to the endosome, thereby preventing it from causing toxicity. A physical interaction between the antidote and the toxin enables the ubiquitinated antidote to translocate the toxin to the endosome and neutralize its toxicity. We propose that post-translational modification-mediated protein localization and/or activity changes may be a common mechanism governing the antagonistic duality of single-gene KMDs.
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