1. The essential role of the N-terminal domain of the orange carotenoid protein in cyanobacterial photoprotection: importance of a positive charge for phycobilisome binding
- Author
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Cheryl A. Kerfeld, Michal Gwizdala, Maxime T. A. Alexandre, Alberto Mezzetti, Diana Kirilovsky, Adjélé Wilson, Commissariat à l'Energie Atomique (CEA), Institut de Biologie et Technologies de Saclay, Systèmes membranaires, photobiologie, stress et détoxification (SMPSD - UMR 8221), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement - UMR 8516 (LASIRE), Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Centrale Lille Institut (CLIL), Department of Physics and Astronomy [Amsterdam], Vrije Universiteit Amsterdam [Amsterdam] (VU), Department of Energy / Joint Genome Institute (DOE), Los Alamos National Laboratory (LANL), Lawrence Berkeley National Laboratory [Berkeley] (LBNL), Berkeley Synthetic Biology Institute [Berkeley] (SYNBIO), University of California [Berkeley], University of California-University of California, Department of Plant and Microbial Biology [Berkeley], Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), University of California [Berkeley] (UC Berkeley), and University of California (UC)-University of California (UC)
- Subjects
0106 biological sciences ,Light ,Lysine ,Plant Science ,Plasma protein binding ,Biology ,Cyanobacteria ,7. Clean energy ,01 natural sciences ,Protein Structure, Secondary ,03 medical and health sciences ,Protein structure ,Bacterial Proteins ,Phycobilisomes ,Research Articles ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,Orange carotenoid protein ,Cell Biology ,Amino acid ,[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry ,Biochemistry ,chemistry ,Photoprotection ,Biophysics ,Phycobilisome ,Salt bridge ,Protein Binding ,010606 plant biology & botany - Abstract
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.
- Published
- 2012
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