Fusion Proteins Containing Proteorhodopsin from Exiguobacterium sibiricum

Petrovskaya, L.E.; Kryukova, E.A.; Bolshakov, V.A.; Lukashev, E.P.; Siletsky, S.A.; Mamedov, M.D.; Sudakov, R.V.; Dolgikh, D.A.; Kirpichnikov, M.P.

Авторы: Petrovskaya L.E., Kryukova E.A., Bolshakov V.A., Lukashev E.P., Siletsky S.A., Mamedov M.D., Sudakov R.V., Dolgikh D.A., Kirpichnikov M.P.
Журнал: Russian Journal of Bioorganic Chemistry
Том: 50
Номер: 3
Год издания: 2024
Издательство: Maik Nauka/Interperiodica Publishing
Местоположение издательства: Russian Federation
Первая страница: 741
Последняя страница: 752
DOI: 10.1134/s1068162024030063
Аннотация: AbstractObjective: To study the transport activity of bacterial rhodopsins, proteoliposomes with the same orientation of the protein molecules should be obtained. Methods: The genes of fusion proteins containing Exiguobacterium sibiricum proteorhodopsin (ESR) and various N-terminal soluble domains have been constructed. Results and Discussion: Effective synthesis in Escherichia coli cells was observed only in the case of fusion with chaperone Caf1M and maltose-binding protein MBP expressed as precursors with their own signal sequences. The study of the isolated MBP-ESR protein in micelles and proteoliposomes demonstrated formation and decay of the main photocycle intermediates at pH > 8. The photoelectric response of the fusion proteins Caf-ESR and MBP-ESR is comparable in amplitude to the wild-type ESR response, indicating their homogeneous orientation in the proteoliposome membrane. Conclusions: The obtained constructs can be used to create bacterial expression systems for various retinal proteins, ensuring their uniform incorporation into proteoliposomes.
Добавил в систему: Силецкий Сергей Алексеевич

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Fusion Proteins Containing Proteorhodopsin from Exiguobacterium sibiricumстатья

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