ATP-Dependent LonBA Proteases of Bacilli and Clostridia

Andrianova, A.G.; Kudzhaev, A.M.; Smirnov, I.V.; Rotanova, T.V.

Авторы: Andrianova A.G., Kudzhaev A.M., Smirnov I.V., Rotanova T.V.
Журнал: Russian Journal of Bioorganic Chemistry
Том: 50
Номер: 5
Год издания: 2024
Издательство: Maik Nauka/Interperiodica Publishing
Местоположение издательства: Russian Federation
Первая страница: 1692
Последняя страница: 1700
DOI: 10.1134/s1068162024050285
Аннотация: Objective: ATP-dependent Lon proteases are key players in the quality control system of cellular proteins. The Lon family includes three main subfamilies (A, B, and C), whose representatives are common in bacteria, eukaryotes, and archaea. Recently, enzymes that potentially form a new “hybrid” subfamily LonBA have been discovered in bacteria of the Bacilli and Clostridia classes. This study aims to characterize the structure of LonBA proteases and elucidate their features by comparison with classical LonA and LonB proteases. Methods: Bioinformatics analysis methods and approaches were used to comparatively characterize Lon proteases of different subfamilies. Results and Discussion: Analysis of sequences of the common pool of Firmiqutes’ Lons showed that they contain both classical LonA and “hybrid” LonBA proteases. The ATPase component of the latters is similar to the ATPase fragment of LonB proteases, while the catalytic P domain is similar to the P domain of LonA proteases. Degrees of similarity of different structural fragments of LonBAs were estimated. Groups of short and long LonBA proteases were identified. Sources of short-LonBAs are both bacilli and clostridia, but long ones—only clostridia. Conclusions: The new subfamily of LonBA proteases was shown to consist of two communities of enzymes that differ in the structure of their N-terminal fragments and protease domains.
Добавил в систему: Бачева Анна Владимировна

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ATP-Dependent LonBA Proteases of Bacilli and Clostridiaстатья