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  • Title: Reversible light activation of the phosphoenolpyruvate carboxylase protein-serine kinase in maize leaves.
    Author: Echevarría C, Vidal J, Jiao JA, Chollet R.
    Journal: FEBS Lett; 1990 Nov 26; 275(1-2):25-8. PubMed ID: 2148159.
    Abstract:
    C4-leaf phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) undergoes reversible, light-induced increases in its activity-seryl phosphorylation-status in vivo. We now report that the PEPC-protein kinase activity in desalted crude extracts of light-adapted maize leaves is several-fold greater than that from the corresponding dark tissue when in vitro phosphorylation assays are performed with either endogenous or purified dark-form maize PEPC as substrate, both in the absence or presence of okadaic acid, a potent inhibitor of the PEPC type 2A protein phosphatase(s). These and related results indicate that the PEPC protein-serine kinase(s) per se is reversibly light activated in vivo by either covalent modification, protein turnover or, less likely, a tight-binding effector.
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