Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
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Karel Müller
Abstract
The effect of viral infection on the regulation of phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) in Nicotiana tabacum L. leaves was studied. PEPC activity was 3 times higher in infected plant leaves compared to healthy plants. Activity of plant PEPC can be regulated, e.g., by de novo synthesis or reversible phosphorylation. The reason for the increase of PEPC activity as a consequence of PVYNTN infection was studied. The amount of PEPC determined by Western blot analysis or by relative estimation of PEPC mRNA by real-time PCR did not differ in control and PVYNTN-infected plants. Changes in post-translational modification of PEPC by phosphorylation were evaluated by comparing activity of the native and the dephosphorylated enzyme. The infected plants were characterized by a higher decrease of the enzyme activity after its dephosphorylation, which indicated a higher phosphorylation level. Immunochemical detection of phosphoproteins by Western blot analysis showed a more intensive band corresponding to PEPC from the infected material. This strengthens the hypothesis of an infection-related phosphorylation, which could be part of the plant's response to pathogen attack. The physiological implications of the increase in PEPC activity during PVYNTN infection are discussed.
©2009 by Walter de Gruyter Berlin New York
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Artikel in diesem Heft
- Review
- Glutathione dysregulation and the etiology and progression of human diseases
- Protein Structure and Function
- Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
- Role of catalytic and non-catalytic subsite residues in ribonuclease activity of human eosinophil-derived neurotoxin
- Cell Biology and Signaling
- Expression and localization of atypical PKC isoforms in liver parenchymal cells
- Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
- The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
- Proteolysis
- Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
- The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
