Heterologous expression and characterization of recombinant OsCDR1, a rice aspartic proteinase involved in disease resistance
| Autor: | Gary Creissen, Bharat B. Chattoo, Bishun Deo Prasad, Chris Lamb |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Antifungal Agents
Aspartic Acid Proteases Recombinant Fusion Proteins medicine.medical_treatment Molecular Sequence Data Arabidopsis Biology medicine.disease_cause law.invention Gene product Gene Expression Regulation Plant Proteinase 3 law Escherichia coli medicine Amino Acid Sequence Glutathione Transferase Plant Proteins chemistry.chemical_classification Protease Temperature food and beverages Oryza Fusion protein Immunity Innate Enzyme chemistry Biochemistry Mutagenesis Site-Directed Recombinant DNA Heterologous expression Biotechnology |
| Zdroj: | Protein Expression and Purification. 72:169-174 |
| ISSN: | 1046-5928 |
| DOI: | 10.1016/j.pep.2010.03.018 |
| Popis: | The Oryza sativa constitutive disease resistance 1 (OsCDR1) gene product is an aspartic proteinase that has been implicated in disease resistance signaling. This apoplastic enzyme is a member of the group of 'atypical' plant aspartic proteinases. Recombinant OsCDR1 expressed in Escherichia coli exhibited protease activity against succinylated-casein substrate. Inactivating the enzyme through modification of an aspartate residue present in the deduced active site completely abolished its proteinase activity. Infiltration of the OsCDR1 fusion protein into leaves of Arabidopsis plants induced PR2 transcripts in both the infiltrated leaf (primary) and in non-treated secondary leaves while the inactive recombinant protein failed to induce either local or systemic PR2. These findings demonstrate that OsCDR1 is capable of inducing systemic defense responses in plants. |
| Databáze: | OpenAIRE |
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