Phosphorylation in vitro of the large subunit of the ribulose-1,5-bisphosphate carboxylase and of the glyceraldehyde-3-phosphate dehydrogenase
| Autor: | Carole Guitton, Régis Mache |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Oxygenase
Ribulose 1 5-bisphosphate Chloroplasts Light Protein subunit Ribulose-Bisphosphate Carboxylase Phosphatase Glyceraldehyde-3-Phosphate Dehydrogenases Biology Darkness Plants Biochemistry Molecular biology Phosphoric Monoester Hydrolases chemistry.chemical_compound chemistry biology.protein Phosphorylation Kinase activity Protein kinase A Protein Kinases Glyceraldehyde 3-phosphate dehydrogenase Plant Proteins |
| Zdroj: | European journal of biochemistry. 166(1) |
| ISSN: | 0014-2956 |
| Popis: | A protein kinase activity responsible for the in vitro phosphorylation of at least six endogenous polypeptides including the large subunit of the ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) is present in the stroma (3000xg supernatant, S30) of spinach chloroplasts. The phosphorylation of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit is strongly enhanced when sodium fluorure is used as a protein phosphatase inhibitor. Phosphorylation occurs on threonine and serine residues. The protein kinase involved is not Ca2+-dependent. There is also evidence for a protein phosphatase activity which suggests a coupled regulation by a phosphorylation-dephosphorylation process. The phosphorylating activity is drastically reduced when S30 is prepared from leaves harvested after a dark period. Phosphorylation of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit is not related to its own synthesis. The in vitro phosphorylation of the glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) is also demonstrated. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text