OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria

Nikolai N. Sluchanko (), Yury B. Slonimskiy, Evgeny A. Shirshin, Marcus Moldenhauer, Thomas Friedrich and Eugene G. Maksimov
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Nikolai N. Sluchanko: Federal Research Center of Biotechnology of the Russian Academy of Sciences
Yury B. Slonimskiy: Federal Research Center of Biotechnology of the Russian Academy of Sciences
Evgeny A. Shirshin: Faculty of Physics, Leninskie gory 1
Marcus Moldenhauer: Institute of Chemistry PC 14
Thomas Friedrich: Institute of Chemistry PC 14
Eugene G. Maksimov: Faculty of Biology, Leninskie gory 1

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-06195-0

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