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The effect of irradiance and redox-modifying reagents on the 52 kDa protein disulfide isomerase of Arabidopsis chloroplasts

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Biologia Plantarum

Abstract

Immunoblot analysis was used to assess the effects of light and redox-modifying chemicals on the 52 kDa protein disulfide isomerase (PDI) from chloroplasts of Arabidopsis thaliana. A monoclonal antiserum was used that preferentially cross-reacts with the 52 kDa relative to the 65 kDa isoform of PDI. The PDI-52 was most abundant in leaves, flowers, stems and seeds, but was undetected in roots. PDI-52 formed a ∼220 kDa protein complex on blue native gels, indicating that it associates with either itself or other proteins in chloroplasts. Light decreased the levels of PDI-52 by 80 %, relative to the control protein (the CF1 subunit of chloroplast ATP synthase). Treatment with dithiothreitol decreased the content of the 52 kDa protein by half. In contrast, when the reduction of plastoquinone is blocked by DCMU, or when the plants are treated with phosphate, PDI-52 contents increased by 1.5 to 2-fold relative to CF1. The effect of the chemical treatments coincided with the effect of the light/dark cycle and implied that light decreased PDI-52 protein content by way of the cellular redox environment.

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Abbreviations

DTT:

dithiothreitol

CF1:

beta subunit of chloroplast ATP synthase

DCMU:

dichlorophenyl)-1,1-dimethylurea

LSU Rubisco:

large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase

PDI:

protein disulfide isomerase

PS:

photosystem

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Correspondence to D. A. Christopher.

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Lu, DP., Christopher, D.A. The effect of irradiance and redox-modifying reagents on the 52 kDa protein disulfide isomerase of Arabidopsis chloroplasts. Biol Plant 52, 42–48 (2008). https://doi.org/10.1007/s10535-008-0006-7

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  • DOI: https://doi.org/10.1007/s10535-008-0006-7

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