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Functional interaction of low-homology FRPs from different cyanobacteria with Synechocystis OCPстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 24 ноября 2018 г.
- Авторы: Slonimskiy Yury B., Maksimov Eugene G., Lukashev Evgeny P., Marcus Moldenhauer, Jeffries Cy M., Svergun Dmitri I., Thomas Friedrich, Sluchanko Nikolai N.
- Журнал: Biochimica et Biophysica Acta - Bioenergetics
- Том: 1859
- Год издания: 2018
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 382
- Последняя страница: 393
- DOI: 10.1016/j.bbabio.2018.03.001
- Аннотация: Photosynthesis requires a balance between efficient light harvesting and protection against photodamage. The cyanobacterial photoprotection system uniquely relies on the functioning of the photoactive orange carotenoid protein (OCP) that under intense illumination provides fluorescence quenching of the light-harvesting antenna complexes, phycobilisomes. The recently identified fluorescence recovery protein (FRP) binds to the photoactivated OCP and accelerates its relaxation into the basal form, completing the regulatory circle. The molecular mechanism of FRP functioning is largely controversial. Moreover, since the available knowledge has mainly been gained from studying Synechocystis proteins, the cross-species conservation of the FRP mechanism remains unexplored. Besides phylogenetic analysis, we performed a detailed structural-functional analysis of two selected low-homology FRPs by comparing them with Synechocystis FRP (SynFRP). While adopting similar dimeric conformations in solution and preserving binding preferences of SynFRP towards various OCP variants, the low homology FRPs demonstrated distinct binding stoichiometries and differentially accentuated features of this functional interaction. By providing clues to understand the FRP mechanism universally, our results also establish foundations for upcoming structural investigations necessary to elucidate the FRP-dependent regulatory mechanism.
- Добавил в систему: Максимов Евгений Георгиевич
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | BBA_2018_FRPs.pdf | 2,4 МБ | 13 марта 2018 [emaksimoff] |