The site of regulation of light capture in Symbiodinium: does the peridinin-chlorophyll a-protein detach to regulate light capture?
Dinoflagellates from the genus Symbiodinium form symbiotic associations with cnidarians including corals and anemones. The photosynthetic apparatuses of these dinoflagellates possess a unique photosynthetic antenna system incorporating the peridinin-chlorophyll a-protein (PCP). It has been proposed that the appearance of a PCP-specific 77K fluorescence emission band around 672-675 nm indicates that high light treatment results in PCP dissociation from intrinsic membrane antenna complexes, blocking excitation transfer to the intrinsic membrane-bound antenna complexes, chlorophyll a-chlorophyll c2-peridinin-protein-complex (acpPC) and associated photosystems (Reynolds et al., 2008 Proc Natl Acad Sci USA 105:13674-13678).We have tested this model using time-resolved fluorescence decay kinetics in conjunction with global fitting to compare the time-evolution of the PCP spectral bands before and after high light exposure. Our results show that no long-lived PCP fluorescence emission components appear either before or after high light treatment, indicating that the efficiency of excitation transfer from PCP to membrane antenna systems remains efficient and rapid even after exposure to high light. The apparent increased relative emission at around 675nm was, instead, caused by strong preferential exciton quenching of the membrane antenna complexes associated with acpPC and reaction centers. This strong non-photochemical quenching (NPQ) is consistent with the activation of xanthophyll-associated quenching mechanisms and the generally-observed avoidance in nature of long-lived photoexcited states that can lead to oxidative damage. The acpPC component appears to be the most strongly quenched under high light exposure suggesting that it houses the photoprotective exciton quencher.
Plant Research Laboratory, R106 Plant Biology Building, Michigan State University, East Lansing, MI 48824-1312, USA. Electronic address: kanazawa@msu.edu.
Atsuko
A
Kanazawa
Department of Chemistry, R328, Michigan State University, East Lansing, MI 48824-1322, USA. Electronic address: Blanchard@chemistry.msu.edu.
Gary J
GJ
Blanchard
Plant Functional Biology and Climate Change Cluster (C3), University of Technology, Sydney, PO Box 123 Broadway, NSW 2007, Australia. Electronic address: Milan.Szabo@uts.edu.au.
Milán
M
Szabó
Plant Functional Biology and Climate Change Cluster (C3), University of Technology, Sydney, PO Box 123 Broadway, NSW 2007, Australia. Electronic address: Peter.Ralph@uts.edu.au.
Peter J
PJ
Ralph
Plant Research Laboratory, R106 Plant Biology Building, Michigan State University, East Lansing, MI 48824-1312, USA. Electronic address: kramerd8@msu.edu.
David M
DM
Kramer
D002338:Carotenoids / Q000737:chemistry / Q000235:genetics*; D004141:Dinoflagellida / Q000235:genetics* / Q000254:growth & development; D004735:Energy Transfer; D005453:Fluorescence; D007700:Kinetics; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry / Q000235:genetics*; D010788:Photosynthesis / Q000235:genetics*; D045332:Photosystem II Protein Complex; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics*
D045342:Light-Harvesting Protein Complexes; D045332:Photosystem II Protein Complex; D015800:Protozoan Proteins; C073227:peridinin chlorophyll-a protein, Dinophyceae; D002338:Carotenoids
Non-photochemical quenching; Peridinin–chlorophyll a–protein; Photoprotection; Photosynthesis