Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease


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Аннотация

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.

Авторлар туралы

A. Andrianova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: tatyana.rotanova@ibch.ru
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997

A. Kudzhaev

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: tatyana.rotanova@ibch.ru
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997

E. Dubovtseva

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: tatyana.rotanova@ibch.ru
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997

T. Rotanova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Хат алмасуға жауапты Автор.
Email: tatyana.rotanova@ibch.ru
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997

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