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

Content Provider	Springer Nature Link
Author	Lu, D. P. Christopher, D. A.
Copyright Year	2008
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.
Starting Page	42
Ending Page	48
Page Count	7
File Format	PDF
ISSN	00063134
Journal	Biologia Plantarum
Volume Number	52
Issue Number	1
e-ISSN	15738264
Language	English
Publisher	Springer Netherlands
Publisher Date	2008-01-01
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Plant Science Horticulture

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