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

来源：

RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY | 2017年 / 43卷 / 04期

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

页码：368 / 376

页数：9

共 28 条

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