ArticleNature communications2018
OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Structure and quenching of a bundle-shaped phycobilisome.Science advances · 2025Article
- Insights into the molecular mechanism of yellow cuticle coloration by a chitin-binding carotenoprotein in gregarious locusts.Communications biology · 2024Article
- Solution Structures of Two Different FRP-OCP Complexes as Revealed via SEC-SANS.International journal of molecular sciences · 2024Article
- Structure and function of the light-protective orange carotenoid protein families.Current research in structural biology · 2024Review
- Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection.Nature ecology & evolution · 2023Article
- Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaP.Communications biology · 2023Article
- Article
- Overview of the "Photoreception" session at the 9th Congress of the Russian Photobiological Society: understanding structure and function of photoreceptors.Biophysical reviews · 2022Article
- Plant adaptability in karst regions.Journal of plant research · 2021Review
- Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein.Communications biology · 2021Article
- Probing of carotenoid-tryptophan hydrogen bonding dynamics in the single-tryptophan photoactive Orange Carotenoid Protein.Scientific reports · 2020Article
- Fluorescence recovery protein: a powerful yet underexplored regulator of photoprotection in cyanobacteria†.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020Review
- A genetically encoded fluorescent temperature sensor derived from the photoactive Orange Carotenoid Protein.Scientific reports · 2019Article
- X-ray radiolytic labeling reveals the molecular basis of orange carotenoid protein photoprotection and its interactions with fluorescence recovery protein.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
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 signals into protein-protein interactions.
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