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Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function

机译:插入的α-螺旋结构域在大肠杆菌ATP依赖的Lon蛋白酶功能中的作用

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摘要

Multidomain ATP-dependent Lon protease of E. coli (Ec-Lon) is one of the key enzymes of the quality control system of the cellular proteome. A recombinant form of Ec-Lon with deletion of the inserted characteristic α-helical HI(CC) domain (Lon-dHI(CC)) has been prepared and investigated to understand the role of this domain. A comparative study of the ATPase, proteolytic, and peptidase activities of the intact Lon protease and Lon-dHI(CC) has been carried out. The ability of the enzymes to undergo autolysis and their ability to bind DNA have been studied as well. It has been shown that the HI(CC) domain of Ec-Lon protease is required for the formation of a functionally active enzyme structure and for the implementation of protein-protein interactions.
机译:大肠杆菌的多域ATP依赖Lon蛋白酶(Ec-Lon)是细胞蛋白质组质量控制系统的关键酶之一。制备了重组形式的Ec-Lon,缺失了插入的特征性α-螺旋HI(CC)域(Lon-dHI(CC)),并进行了研究以了解该域的作用。已对完整的Lon蛋白酶和Lon-dHI(CC)的ATPase,蛋白水解和肽酶活性进行了比较研究。还研究了酶进行自溶的能力及其结合DNA的能力。已经显示,Ec-Lon蛋白酶的HI(CC)结构域对于形成功能活性酶结构和实现蛋白质-蛋白质相互作用是必需的。

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