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Plant Physiology 65:730-734 (1980)
© 1980 American Society of Plant Biologists

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A Light-dependent Protein Kinase Activity of Chloroplasts 1,2

Ramona Alfonzo3, Nathan Nelson4 and Efraim Racker

Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853

A protein kinase activity from spinach chloroplasts, tightly associated with the thylakoid membranes, has been solubilized and partially characterized. This membrane-bound protein kinase is stimulated by light and electron transport activity through photosystem II appears to be required for stimulation.

Electron transport inhibitors like 3,4-dichlorophenyl-1,1-dimethylurea, Tris, and NH2OH treatments, inhibit the light activation process. Furthermore, after Tris inhibition, the protein kinase activity is restored by washing the Tris-treated chloroplasts with dichlorophenol indophenol plus ascorbate. The protein kinase remains active in the dark after short illumination periods, suggesting that a product of electron transport may be involved in light activation.

Two endogenous substrates of the protein kinase in thylakoid membranes are the N,N'-dicyclohexylcarbodiimide-reactive proteolipid and the light-harvesting chlorophyll-protein complex. The membrane-bound protein kinase also phosphorylates externally added histone.

3 This research was done as a partial fulfillment of the requirements for the Ph.D. degree at Cornell University.

4 Present address: Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.

1 This investigation was supported by Grant BMS-17887 from the National Science Foundation and Consejo de Desarrollo Cientifico y Humanistico Universidad Central de Venezuela.

2 Dedicated to the memory of Dr. Bessel Kok.






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