Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation

Photosynthetic cyanobacteria make important contributions to global carbon and nitrogen budgets. A protein known as the orange carotenoid protein (OCP) protects the photosynthetic apparatus from damage by dissipating excess energy absorbed by the phycobilisome, the major light-harvesting complex in...

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Veröffentlicht in:Biochemistry (Easton) 2016-02, Vol.55 (7), p.1003-1009
Hauptverfasser: Liu, Haijun, Zhang, Hao, Orf, Gregory S, Lu, Yue, Jiang, Jing, King, Jeremy D, Wolf, Nathan R, Gross, Michael L, Blankenship, Robert E
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container_end_page 1009
container_issue 7
container_start_page 1003
container_title Biochemistry (Easton)
container_volume 55
creator Liu, Haijun
Zhang, Hao
Orf, Gregory S
Lu, Yue
Jiang, Jing
King, Jeremy D
Wolf, Nathan R
Gross, Michael L
Blankenship, Robert E
description Photosynthetic cyanobacteria make important contributions to global carbon and nitrogen budgets. A protein known as the orange carotenoid protein (OCP) protects the photosynthetic apparatus from damage by dissipating excess energy absorbed by the phycobilisome, the major light-harvesting complex in many cyanobacteria. OCP binds one carotenoid pigment, but the color of this pigment depends on conditions. It is orange in the dark and red when exposed to light. We modified the orange and red forms of OCP by using isotopically coded cross-linking agents and then analyzed the structural features by using liquid chromatography and tandem mass spectrometry. Unequivocal cross-linking pairs uniquely detected in red OCP indicate that, upon photoactivation, the OCP N-terminal domain (NTD) and C-terminal domain (CTD) reorient relative to each other. Our data also indicate that the intrinsically unstructured loop connecting the NTD and CTD not only is involved in the interaction between the two domains in orange OCP but also, together with the N-terminal extension, provides a structural buffer system facilitating an intramolecular breathing motion of the OCP, thus helping conversion back and forth from the orange to red form during the OCP photocycle. These results have important implications for understanding the molecular mechanism of action of cyanobacterial photoprotection.
doi_str_mv 10.1021/acs.biochem.6b00013
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subjects Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
BASIC BIOLOGICAL SCIENCES
Carotenoids - chemistry
Carotenoids - metabolism
Carotenoids - radiation effects
Chromatography, High Pressure Liquid
Cross-Linking Reagents - chemistry
Dimerization
Ligands
Light
Models, Molecular
Molecular Weight
Peptide Mapping
Photochemical Processes
Photosynthesis
Protein Refolding - radiation effects
Protein Structure, Tertiary - radiation effects
solar (fuels), photosynthesis (natural and artificial), biofuels (including algae and biomass), bio-inspired, charge transport, membrane, synthesis (novel materials), synthesis (self-assembly)
Synechocystis - metabolism
Tandem Mass Spectrometry
title Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation
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