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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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Expression of Xanthorhodopsin in Escherichia coliстатья
- Авторы: Petrovskaya Lada E., Lukashev Evgeniy P., Lyukmanova Ekaterina N., Shulepko Mikhail A., Kryukova Elena A., Ziganshin Rustam H., Dolgikh Dmitriy A., Maksimov Evgeniy G., Rubin Andrei B., Kirpichnikov Mikhail P., Lanyi Janos K., Balashov Sergei P.
- Журнал: Protein Journal
- Год издания: 2023
- Издательство: Springer Verlag
- Местоположение издательства: Germany
- DOI: 10.1007/s10930-023-10109-5
- Аннотация: Xanthorhodopsin (XR) from Salinibacter ruber is a light-driven proton pump containing retinal and a light-harvesting carotenoid antenna salinixanthin. Previous structure-functional studies of XR were conducted using a protein isolated from the native host only due to the absence of heterologous expression in Escherichia coli. In this paper, we describe cell-free synthesis and incorporation in lipid–protein nanodiscs of the recombinant XR that demonstrated its principal compatibility with E. coli biosynthetic machinery. To produce XR in E. coli, three C-terminal deletion variants of this protein were constructed. In contrast to the full-length XR, their expression resulted in efficient synthesis in E. coli cells. However, cells producing recombinant XR variants bound retinal only upon growth in minimal medium, not in the rich one. The XR3 variant with deletion of ten C-terminal amino acid residues was obtained and characterized. Its absorption spectrum and photocycle kinetics were close to those reported for XR isolated from S. ruber membranes and bleached from salinixanthin. We have also constructed the first mutants of XR, H62M and D96N, and examined their properties.
- Добавил в систему: Максимов Евгений Георгиевич
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | s10930-023-10109-5.pdf | s10930-023-10109-5.pdf | 1,8 МБ | 25 августа 2023 [evgenylukashev] |