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Life Sciences Commons

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Biochemistry, Biophysics, and Structural Biology

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University of Nebraska - Lincoln

1991

Light activation

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Full-Text Articles in Life Sciences

Protein Turnover As A Component In The Light/Dark Regulation Of PhosphoEnolPyruvate Carboxylase Protein-Serine Kinase Activity In C4 Plants, Jin-An Jiao, Cristina Echevarría, Jean Vidal, Raymond Chollet Jan 1991

Protein Turnover As A Component In The Light/Dark Regulation Of PhosphoEnolPyruvate Carboxylase Protein-Serine Kinase Activity In C4 Plants, Jin-An Jiao, Cristina Echevarría, Jean Vidal, Raymond Chollet

Department of Biochemistry: Faculty Publications

Maize leaf phosphoenolpyruvate carboxylase [PEPC; orthophosphate:oxaloacetate carboxy-lyase (phosphorylating), EC 4.1.1.311 protein-serine kinase (PEPC-PK) phosphorylates serine-15 of its target enzyme, thus leading to an increase in catalytic activity and a concomitant decrease in malate sensitivity of this cytoplasmic C4 photosynthesis enzyme in the light. We have recently demonstrated that the PEPC-PK activity in maize leaves is slowly, but strikingly, increased in the light and decreased in darkness. In this report, we provide evidence that cycloheximide, an inhibitor of cytoplasmic protein synthesis, when fed to detached leaves of C4 monocots (maize, sorghum) and dicots (Portulaca oleracea) in the …