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<p>Embryogenesis in plants is a complex process, and proteins encoded by genes that affect embryo development in maize are typically localized in plastids. In this study, we isolated a maize embryo-specific defective mutant (<i>emb</i>) in which the mutant embryos were arrested at the transition stage and the endosperm size was reduced compared to the wild type (WT). The grain-filling rate of <i>zmcfm1</i> was significantly lower than that of the WT, resulting in a markedly reduced weight of mature grains. The mutant gene <i>ZmCFM1</i> was identified by bulked segregant analysis sequencing and map-based cloning. <i>ZmCFM1</i> encodes a plastid-localized CRM family protein involved in the splicing of group II introns in plastids. The splicing efficiency of the <i>trnA</i>, <i>trnI</i>, <i>trnK</i>, <i>trnV</i>, and <i>rpl2</i> introns in the plastids of <i>zmcfm1</i> was significantly reduced. The impairment of intron splicing disrupts ribosome assembly and plastid protein translation, ultimately causing embryo arrest and lethality.</p>

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Maize CRM-domain family protein CFM1 regulates kernel development via plastid group II intron splicing

  • 期刊论文

  • 发表日期：

    2026年2月26日

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  • Xuewu He,
  • Huayang Lv,
  • Zeting Mou,
  • Xuerui He,
  • Hongyu Zhang,
  • Dianyuan Cai,
  • Hanmei Liu,
  • Yangping Li,
  • Yufeng Hu,
  • Yinghong Liu,
  • Yubi Huang,
  • Junjie Zhang

摘要

Embryogenesis in plants is a complex process, and proteins encoded by genes that affect embryo development in maize are typically localized in plastids. In this study, we isolated a maize embryo-specific defective mutant (emb) in which the mutant embryos were arrested at the transition stage and the endosperm size was reduced compared to the wild type (WT). The grain-filling rate of zmcfm1 was significantly lower than that of the WT, resulting in a markedly reduced weight of mature grains. The mutant gene ZmCFM1 was identified by bulked segregant analysis sequencing and map-based cloning. ZmCFM1 encodes a plastid-localized CRM family protein involved in the splicing of group II introns in plastids. The splicing efficiency of the trnA, trnI, trnK, trnV, and rpl2 introns in the plastids of zmcfm1 was significantly reduced. The impairment of intron splicing disrupts ribosome assembly and plastid protein translation, ultimately causing embryo arrest and lethality.