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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Cysteine protease mcll-Pa executes programmed cell death during plant embryogenesis
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Cysteine protease mcll-Pa executes programmed cell death during plant embryogenesis

机译：半胱氨酸蛋白酶mcll-Pa在植物胚胎发生期间执行程序性细胞死亡

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摘要

Programmed cell death (PCD) is indispensable for eukaryotic development. In animals, PCD is executed by the caspase family of cysteine proteases. Plants do not have close homologues of caspases but possess a phylogenetically distant family of cysteine proteases named metacaspases. The cellular function of metacaspases in PCD is unknown. Here we show that during plant embryogenesis, metacaspase mcII-Pa translocates from the cytoplasm to nuclei in terminally differentiated cells that are destined for elimination, where it colocalizes with the nuclear pore complex and chromatin, causing nuclear envelope disassembly and DNA fragmentation. The cell-death function of mcII-Pa relies on its cysteine-dependent arginine-specific proteolytic activity. Accordingly, mutation of catalytic cysteine abrogates the proteolytic activity of mcII-Pa and blocks nuclear degradation. These results establish metacaspase as an executioner of PCD during embryo patterning and provide a functional link between PCD and embryogenesis in plants. Although mcII-Pa and metazoan caspases have different substrate specificity, they serve a common function during development, demonstrating the evolutionary parallelism of PCD pathways in plants and animals.
机译：程序性细胞死亡（PCD）对于真核细胞发育是必不可少的。在动物中，PCD由半胱氨酸蛋白酶的胱天蛋白酶家族执行。植物没有半胱氨酸蛋白酶的紧密同源物，但是拥有一个在系统发育上远缘的半胱氨酸蛋白酶家族，称为半胱氨酸蛋白酶。在PCD中metacaspases的细胞功能尚不清楚。在这里，我们显示出在植物胚胎发生过程中，metaspaspase mcII-Pa在最终分化的细胞中从细胞质转移到细胞核，该细胞最终被消除，并与核孔复合物和染色质共定位，从而导致核被膜解体和DNA断裂。 mcII-Pa的细胞死亡功能取决于其半胱氨酸依赖性的精氨酸特异性蛋白水解活性。因此，催化半胱氨酸的突变消除了mcII-Pa的蛋白水解活性并阻止了核降解。这些结果建立了metaspaspase作为PCD在胚胎形成过程中的执行者，并提供了PCD与植物胚发生之间的功能联系。尽管mcII-Pa和后生半胱天冬酶具有不同的底物特异性，但它们在发育过程中起着共同的作用，证明了动植物PCD途径的进化平行性。

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