The essential role of the N-terminal domain of the orange carotenoid protein in cyanobacterial photoprotection: importance of a positive charge for phycobilisome binding.
Most cyanobacteria, under high light conditions, decrease the amount of energy arriving at the reaction centers by increasing thermal energy dissipation at the level of the phycobilisome, the extramembranous antenna. This mechanism is induced by photoactivation of the Orange Carotenoid Protein (OCP). To identify how the activated OCP interacts with phycobilisomes (PBs), several OCP mutants were constructed, and the influence of mutations on photoactivity, stability, and binding to PBs was characterized. The disruption of the salt bridge between Arg155 and Glu244, which stabilizes the interaction between the N- and C-terminal domains, increased the rate of photoactivity and the stability of the photoactivated OCP, suggesting that the activated OCP has an open structure with decreased interdomain interaction. Changing Glu244 to leucine had no effect on OCP binding to PBs. By contrast, substitution of Arg155 with a neutral or a negatively charged amino acid largely decreased OCP binding to the PBs, whereas substitution with a lysine slightly perturbed the interaction. These results strongly suggest that the surface of the N-terminal domain, containing the Arg155, interacts with the PB and that the positive charge of Arg155 plays a key role in photoprotection.
Commissariat à l'Energie Atomique, Institut de Biologie et Technologies de Saclay, 91191 Gif sur Yvette, France.
Adjélé
A
Wilson
Michal
M
Gwizdala
Alberto
A
Mezzetti
Maxime
M
Alexandre
Cheryl A
CA
Kerfeld
Diana
D
Kirilovsky
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D000458:Cyanobacteria / Q000187:drug effects / Q000378:metabolism*; D008027:Light; D045524:Phycobilisomes / Q000494:pharmacology*; D011485:Protein Binding; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D045524:Phycobilisomes; C109473:orange carotenoid protein, Synechocystis