Involvement of the N-Terminal Region and Its Characteristic Coiled-Coil Fragment in the Function and Structure Maintenance of E-coli LonA Protease

被引:4
|
作者
Andrianova, A. G. [1 ]
Kudzhaev, A. M. [1 ]
Dubovtseva, E. S. [1 ]
Rotanova, T. V. [1 ]
机构
[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Ul Miklukho Maklaya 16-10, Moscow 117997, Russia
基金
俄罗斯科学基金会;
关键词
AAA(+) proteins; LonA proteases; ATP-dependent proteolysis; role of N-terminal region; ATP-DEPENDENT PROTEASES; QUALITY CONTROL; LIMITED PROTEOLYSIS; DOMAIN; CLASSIFICATION; CHAPERONES; ATPASES; BINDING;
D O I
10.1134/S1068162017040021
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The truncated form of E. coli LonA protease (EcLon) lacking the N-terminal fragment 1-172 (Lon173) and the variant with deleted coiled-coil (CC) fragment 173-283 (dCC-Lon, a deletion form) are produced and characterized to study the role of the N-terminal region in the functioning of this protease. A comparative analysis of the properties of full-length EcLon protease, dCC-Lon, and Lon173 as well as an earlier produced form with retained C-terminal region (235-280) of CC fragment, Lon235, is performed. As is shown, fragment 1-280 plays an important role in both formation of the ATPase site and maintenance of a stable EcLon protease conformation. Fragment 107-172 is of a paramount importance for implementation of the processive mechanism of ATP-dependent proteolysis.
引用
收藏
页码:368 / 376
页数:9
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