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OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteriaстатья Исследовательская статья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Nikolai Sluchanko, Yury Slonimskiy, Evgeny Shirshin, Marcus Moldenhauer, Thomas Friedrich, Eugene Maksimov
- Журнал: Nature communications
- Год издания: 2018
- Издательство: Nature Pub. Group
- Местоположение издательства: United Kingdom
- DOI: 10.1038/s41467-018-06195-0
- Аннотация: In cyanobacteria, high light photoactivates the Orange Carotenoid Protein (OCP) that binds to antennae complexes, dissipating energy and preventing the destruction of the photosynthetic apparatus. At low light, OCP is efficiently deactivated by a poorly understood action of the dimeric Fluorescence Recovery Protein (FRP). Here, we engineer FRP variants with defined oligomeric states and scrutinize their functional interaction with OCP. Complemented by disulfide trapping and chemical crosslinking, structural analysis in solution reveals the topology of metastable complexes of OCP and the FRP scaffold with different stoichiometries. Unable to tightly bind monomeric FRP, photoactivated OCP recruits dimeric FRP, which subsequently monomerizes giving 1:1 complexes. This could be facilitated by a transient OCP–2FRP–OCP complex formed via the two FRP head domains, significantly improving FRP efficiency at elevated OCP levels. By identifying key molecular interfaces, our findings may inspire the design of optically triggered systems transducing light signal into protein-protein interactions.
- Добавил в систему: Максимов Евгений Георгиевич
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