<p>Transcriptional repression is a central mechanism regulating plant growth and development, yet how plant-specific corepressors achieve robust gene silencing remains unclear. Here, we identify the rice corepressor TPR2 (TOPLESS-RELATED 2) as a phase-separating protein that forms nuclear condensates through the cooperative action of an intrinsically disordered region (IDR1) and a plant-specific N-terminal tetramerization domain. Structure-guided mutagenesis disrupting tetramerization or deleting IDR1 markedly impaired condensate formation in vivo and in vitro. Complementation assays showed that only full-length TPR2, capable of robust condensate formation, rescued the growth defects of the <i>tpr2</i> mutant, whereas phase separation-deficient variants failed to do so. Mechanistically, we demonstrate that TPR2 co-condenses with repressors such as D53 and IAA3 to facilitate histone deacetylation and establish repressive chromatin states in a phase separation-dependent manner, thereby fine-tuning key developmental genes. Together, these findings define a condensate-based mechanism for transcriptional repression in plants, linking corepressor phase separation to chromatin modification, gene silencing and developmental control.</p>

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The TPR2 corepressor forms condensates with repressors to fine-tune growth and development in rice

  • Yu Zhang,
  • Bingchen Li,
  • Yu Chen,
  • Jiawei Li,
  • Yao Wang,
  • Tiantian Ye,
  • Ying Ye,
  • Zhiwei Liu,
  • Zhiyue Feng,
  • Stephanie Hutin,
  • Shaoli Zhou,
  • Jianping Guo,
  • Ruihui Zhang,
  • Zhu Liu,
  • Faming Dong,
  • Haiyan Xiong,
  • Chloe Zubieta,
  • Lizhong Xiong,
  • Xuelei Lai

摘要

Transcriptional repression is a central mechanism regulating plant growth and development, yet how plant-specific corepressors achieve robust gene silencing remains unclear. Here, we identify the rice corepressor TPR2 (TOPLESS-RELATED 2) as a phase-separating protein that forms nuclear condensates through the cooperative action of an intrinsically disordered region (IDR1) and a plant-specific N-terminal tetramerization domain. Structure-guided mutagenesis disrupting tetramerization or deleting IDR1 markedly impaired condensate formation in vivo and in vitro. Complementation assays showed that only full-length TPR2, capable of robust condensate formation, rescued the growth defects of the tpr2 mutant, whereas phase separation-deficient variants failed to do so. Mechanistically, we demonstrate that TPR2 co-condenses with repressors such as D53 and IAA3 to facilitate histone deacetylation and establish repressive chromatin states in a phase separation-dependent manner, thereby fine-tuning key developmental genes. Together, these findings define a condensate-based mechanism for transcriptional repression in plants, linking corepressor phase separation to chromatin modification, gene silencing and developmental control.