Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease
- Authors: Andrianova A.G.1, Kudzhaev A.M.1, Dubovtseva E.S.1, Rotanova T.V.1
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Affiliations:
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
- Issue: Vol 43, No 4 (2017)
- Pages: 368-376
- Section: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/228574
- DOI: https://doi.org/10.1134/S1068162017040021
- ID: 228574
Cite item
Abstract
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.
About the authors
A. G. Andrianova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Miklukho-Maklaya 16/10, Moscow, 117997
A. M. Kudzhaev
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Miklukho-Maklaya 16/10, Moscow, 117997
E. S. Dubovtseva
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Miklukho-Maklaya 16/10, Moscow, 117997
T. V. Rotanova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Author for correspondence.
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Miklukho-Maklaya 16/10, Moscow, 117997