Abstract
In higher plants the light energy is captured by the photosynthetic pigments that are bound to photosystem I and II and their light-harvesting complex (LHC) subunits. In this study, we examined the photodynamic changes within chlorophyll-protein complexes in the thylakoid membrane of Arabidopsis thaliana leaves adapted to low light and subsequently exposed to light stress. Chlorophyll-protein complexes were isolated using sucrose density gradient centrifugation and blue-native polyacrylamid gel electrophoresis (BN-PAGE). Proteome analysis was performed using SDS-PAGE, HPLC, and high resolution mass spectrometry. We identified several rarely expressed and stress-induced chlorophyll-binding proteins, showed changes in localization of early light-induced protein family and LHC protein family members between different photosynthetic complexes and assembled/disassembled subcomplexes under light stress conditions and discuss their role in a variety of light stress-related processes.
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Abbreviations
- BN:
-
blue-native
- CID:
-
collision-induced dissociation
- DM:
-
N-dodecyl-β-D-maltoside
- FTICR-MS:
-
Fourier transform ion cyclotron resonance mass spectrometry
- HL:
-
high light
- LHC:
-
light-harvesting complex
- LL:
-
low light
- MALDI:
-
matrix assisted laser desorption/ionisation
- PSI and PSII:
-
photosystem I and II, respectively
- ROS:
-
reactive oxygen species
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Galetskiy, D.N., Lohscheider, J.N., Kononikhin, A.S. et al. Light stress photodynamics of chlorophyll-binding proteins in Arabidopsis thaliana thylakoid membranes revealed by high-resolution mass spectrometric studies. Russ J Bioorg Chem 37, 105–118 (2011). https://doi.org/10.1134/S1068162011010079
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DOI: https://doi.org/10.1134/S1068162011010079