Molecular bases of an alternative dual-enzyme system for light color acclimation of marine <i>Synechococcus</i> cyanobacteria
Théophile Grébert, Adam A. Nguyen, Suman Pokhrel, Kes Lynn Joseph, Morgane Ratin, Louison Dufour, Bo Chen, Allissa M. Haney, Jonathan A. Karty, Jonathan C. Trinidad, Laurence Garczarek, Wendy M. Schluchter, David M. Kehoe, Frédéric Partensky
Abstract
sp. strain A15-62 and demonstrate their critical role in CA4-B. While MpeW, encoded in the CA4-B island and up-regulated in green light, attaches the green light-absorbing chromophore phycoerythrobilin to cysteine-83 of the PEII α-subunit in green light, MpeQ binds phycoerythrobilin and isomerizes it into the blue light-absorbing phycourobilin at the same site in blue light, reversing the relationship of MpeZ and MpeY in the CA4-A strain RS9916. Our data thus reveal key molecular differences between the two types of chromatic acclimaters, both highly abundant but occupying distinct complementary ecological niches in the ocean. They also support an evolutionary scenario whereby CA4-B island acquisition allowed former blue light specialists to become chromatic acclimaters, while former green light specialists would have acquired this capacity by gaining a CA4-A island.