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Published on: September 28, 2013
Light-mediated changes in two proteins found associated with plasma membrane fractions from pea stem sections
S Gallagher1, T W Short, P M Ray
1Department of Biological Sciences, Stanford University, Stanford, CA 94305.
Summary
White light irradiation of pea seedlings affects two plasma membrane proteins. One protein is phytochrome, while the other is a phosphorylatable protein, with both decreasing after light exposure.
Area of Science:
- Plant biology
- Molecular plant science
- Photobiology
Background:
- Plasma membranes are crucial for plant cell signaling.
- Phytochrome is a key photoreceptor in plants.
- Protein phosphorylation plays a role in signal transduction.
Purpose of the Study:
- To investigate the effects of light irradiation on pea seedling plasma membrane proteins.
- To identify and characterize proteins associated with the plasma membrane.
- To understand the differential responses of these proteins to various light conditions.
Main Methods:
- Isolation of plasma membrane fractions from pea seedlings.
- In vitro phosphorylation assays using exogenous ATP.
- Electrophoretic transfer (Western) blot analysis using antibodies against phytochrome.
- Sucrose gradient centrifugation to analyze protein distribution.
- Differential light treatments (white, red, blue light) before irradiation.
Main Results:
- Two proteins near 120 kDa were identified in plasma membrane fractions.
- One protein was identified as phytochrome, and the other as a phosphorylatable protein.
- Both phytochrome and the phosphorylatable protein decreased upon white light irradiation.
- Blue light significantly reduced phosphorylation signal, while red light primarily affected phytochrome levels.
- Evidence suggests the phosphorylatable protein is distinct from phytochrome.
Conclusions:
- Pea seedling plasma membranes contain both phytochrome and a distinct phosphorylatable protein.
- Light irradiation, particularly blue light, differentially affects these two proteins.
- The precise mechanism of blue light-induced decline in phosphorylation requires further investigation.

