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Cyanobacteriochromes are a newly recognized group of photoreceptors that are distinct relatives of phytochromes but are found only in cyanobacteria. A putative cyanobacteriochrome, CcaS, is known to chromatically regulate the expression of the phycobilisome linker gene (cpcG2 ) inSynechocystis sp. PCC 6803. In this study, we isolated the chromophore-binding domain of CcaS fromSynechocystis as well as from phycocyanobilin-producingEscherichia coli . Both preparations showed the same reversible photoconversion between a green-absorbing form (Pg, λmax = 535 nm) and a red-absorbing form (Pr, λmax = 672 nm). Mass spectrometry and denaturation analyses suggested that Pg and Pr bind phycocyanobilin in a double-bond configuration of C15-Z and C15-E , respectively. Autophosphorylation activity of the histidine kinase domain in nearly full-length CcaS was up-regulated by preirradiation with green light. Similarly, phosphotransfer to the cognate response regulator, CcaR, was higher in Pr than in Pg. From these results, we conclude that CcaS phosphorylates CcaR under green light and induces expression ofcpcG2 , leading to accumulation of CpcG2-phycobilisome as a chromatic acclimation system. CcaS is the first recognized green light receptor in the expanded phytochrome superfamily, which includes phytochromes and cyanobacteriochromes.

Cyanobacteriochrome CcaS is the green light receptor that induces the expression of phycobilisome linker protein