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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana
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Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana

机译:结构了解植物细胞程序性死亡由包在拟南芥蛋白质芥

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The recently identified plant Bcl-2-associated athanogene (BAG) family plays an extensive role in plant programmed cell death (PCD) processes ranging from growth and development to stress responses and even cell death. In the Arabidopsis thaliana BAG (AtBAG) protein family, four members (AtBAG1-4) have a domain organization similar to that of mammalian BAG proteins. Here, crystal structures of the BAG domains (BDs) of AtBAG1-4 have been determined; they have high homology and adopt a structure comprising three short parallel α-helices, similar to some mammalian BAG proteins. The crystal structure of a complex of the AtBAG1 ubiquitin-like domain and BAG domain (UBD) with the Hsc70 nucleotide-binding domain (NBD) was also determined. The binding of the AtBAG1 BD to the Hsc70 NBD induces conformational change of the Hsc70 NBD to the open state and reduces the affinity of the NBD for ADP. In vivo studies showed that bag2-1 mutant plants are larger than wild-type plants when growing under normal conditions, indicating that the AtBAG proteins might regulate plant PCD and confer tolerance to stresses in plants. These structural and functional analyses indicate that the AtBAG proteins function as nucleotide-exchange factors for Hsp70/Hsc70 in A. thaliana and that the mechanism of regulation of chaperone-mediated protein folding is conserved in plants.
机译:最近发现植物Bcl-2-associatedathanogene(袋)家庭中起着广泛的作用在植物细胞程序性死亡(PCD)的过程从对压力的增长和发展甚至细胞死亡的反应。芥袋(AtBAG)蛋白家族,四个成员(AtBAG1-4)域组织类似哺乳动物袋的蛋白质。包的结构域(BDs) AtBAG1-4已经确定;采用并行结构包括三个短α螺旋,类似于一些哺乳动物袋蛋白质。域的AtBAG1 ubiquitin-like域和包(钻井)Hsc70 nucleotide-binding域(NBD)也确定。AtBAG1 BD Hsc70 NBD引起构象改变Hsc70 NBD的开放状态降低了ADP NBD的亲和力。研究表明,bag2-1变异植物比野生型植物生长在正常情况下,表明AtBAG蛋白质可能调节植物PCD和授予宽容在植物压力。和功能分析表明AtBAG蛋白质功能nucleotide-exchange因素对Hsp70 / Hsc70芥,即使伴娘的监管机制在植物蛋白质折叠是守恒的。

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