拟南芥AtTR1对AtCPK28和AtCPK32的体外泛素化修饰研究
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Q816

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国家自然科学基金


Investigation on ubiquitination of AtCPK28 and AtCPK32 by AtTR1 in vitro
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    摘要:

    AtTR1、AtCPK28、AtCPK32是参与非生物胁迫应答的相关蛋白,并且与Ca2+信号通路密切关联。为了分析AtTR1和AtCPK28、AtCPK32之间关系,在大肠杆菌中表达了AtTR1、AtCPK28和AtCPK32基因,纯化了表达蛋白,并在体外研究了AtTR1对AtCPK28和AtCPK32泛素化作用,结果发现AtTR1在体外能够对AtCPK28和AtCPK32进行多泛素化修饰。该结果表明AtCPK28和AtCPK32可能是AtTR1调控植物抗逆信号中的下游靶蛋白。该研究结果不仅为进一步研究AtTR1与AtCPK28和AtCPK32之间的相互作用提供了实验证据,而且为研究三者在植物非生物胁迫中的分子机制奠定了基础。

    Abstract:

    AtTR1, AtCPK28, and AtCPK32 are functioning in the abiotic stress response in Arabidopsis thialiana, and closely associated with the calcium signaling pathway. In order to analyze relationships between AtTR1, AtCPK28 and AtCPK32, we expressed AtTR1, AtCPK28, and AtCPK32 in Escherichia coli, purified expression proteins, and studied the ubiquitination of AtCPK28 and AtCPK32 by AtTR1 in vitro. The results showed that the AtCPK28 and AtCPK32 were multi-ubiquitylated by AtTR1 in vitro. It indicated that the AtCPK28 and AtCPK32 are potential downstream targets of AtTR1 in the regulation of stress resistance signaling pathways. These findings provided experimental evidence to further study the interactions between AtTR1, AtCPK28, and AtCPK32, and also provided some insights of their molecular mechanisms in the plant under abiotic stresses.

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引用本文格式: 樊莉娟,陈彩丽,朱旭辉,黄奎,姚润东,王健美. 拟南芥AtTR1对AtCPK28和AtCPK32的体外泛素化修饰研究[J]. 四川大学学报: 自然科学版, 2017, 54: 617.

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历史
  • 收稿日期:2016-01-21
  • 最后修改日期:2016-05-05
  • 录用日期:2016-05-05
  • 在线发布日期: 2017-06-03
  • 出版日期: