A primordial Orange Carotenoid Protein: Structure, photoswitching activity and evolutionary aspects

Slonimskiy, Y.B.; Zupnik, A.O.; Varfolomeeva, L.A.; Boyko, K.M.; Maksimov, E.G.; Sluchanko, N.N.

Авторы: Slonimskiy Yury B., Zupnik Andrei O., Varfolomeeva Larisa A., Boyko Konstantin M., Maksimov Eugene G., Sluchanko Nikolai N.
Журнал: International Journal of Biological Macromolecules
Том: 222
Год издания: 2022
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Первая страница: 167
Последняя страница: 180
DOI: 10.1016/j.ijbiomac.2022.09.131
Аннотация: Cyanobacteria are photosynthesizing prokaryotes responsible for the Great Oxygenation Event on Earth ~2.5 Ga years ago. They use a specific photoprotective mechanism based on the 35-kDa photoactive Orange Carotenoid Protein (OCP), a promising target for developing novel optogenetic tools and for biomass engineering. The two-domain OCP presumably stems from domain fusion, yet the primitive thylakoid-less cyanobacteria Gloeobacter encodes a complete OCP. Its photosynthesis regulation lacks the so-called Fluorescence Recovery Protein (FRP), which in Synechocystis inhibits OCP-mediated phycobilisome fluorescence quenching, and Gloeobacter OCP belongs to the recently defined, heterogeneous clade OCPX (GlOCPX), the least characterized compared to OCP2 and especially OCP1 clades. Here, we describe the first crystal structure of OCPX, which explains unique functional adaptations of Gloeobacter OCPX compared to OCP1 from Synechocystis. We show that monomeric GlOCPX exploits a remarkable intramolecular locking mechanism stabilizing its dark-adapted state and exhibits drastically accelerated, less temperature-dependent recovery after photoactivation. While GlOCPX quenches Synechocystis phycobilisomes similar to Synechocystis OCP1, it evades interaction with and regulation by FRP from other species and likely uses alternative mechanisms for fluorescence recovery. This analysis of a primordial OCPX sheds light on its evolution, rationalizing renaming and subdivision of the OCPX clade into subclades – OCP3a, OCP3b, OCP3c.
Добавил в систему: Максимов Евгений Георгиевич

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A primordial Orange Carotenoid Protein: Structure, photoswitching activity and evolutionary aspectsстатья

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