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. 1980 Apr;65(4):730–734. doi: 10.1104/pp.65.4.730

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

Ramona Alfonzo 1,3, Nathan Nelson 1,4, Efraim Racker 1
PMCID: PMC440413  PMID: 16661269

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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