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Light stress photodynamics of chlorophyll-binding proteins in Arabidopsis thaliana thylakoid membranes revealed by high-resolution mass spectrometric studies

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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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Correspondence to E. N. Nikolaev.

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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

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