Reversible light activation of the phosphoenolpyruvate carboxylase protein‐serine kinase in maize leaves

FEBS Letters

Vidal, Jean¹  Chollet, Raymond¹  Echevarría, Cristina¹  Jiao, Jin-an¹ 

[1] Department of Biochemistry, University of Nebraska-Lincoln, East Campus, Lincoln, Nebraska 68583-0718, USA

关键词: Phosphoenolpyruvate carboxylase;    Protein-serine kinase;    Regulatory protein phosphorylation;    C4 photosynthesis;    Light-dark regulation;    Maize (Zea mays L.);   

DOI  :  10.1016/0014-5793(90)81430-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

C ₄-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 endogeneous 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, less likely, a tight-binding effector.

【 授权许可】

Unknown