Heterologous expression and characterization of recombinant OsCDR1, a rice aspartic proteinase involved in disease resistance

Deo Prasad, Bishun ; Creissen, Gary ; Lamb, Chris ; Chattoo, Bharat B. (2010) Heterologous expression and characterization of recombinant OsCDR1, a rice aspartic proteinase involved in disease resistance Protein Expression and Purification, 72 (2). pp. 169-174. ISSN 1046-5928

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.pep.2010.03.018

Abstract

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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Oryza sativa Constitutive Disease Resistance 1 (OsCDR1); Aspartic Proteinase (AP); Salicylic Acid (SA); Pathogenesis-related (PR) Gene; Glutathione-S-transferase (GST)
ID Code:60116
Deposited On:08 Sep 2011 10:01
Last Modified:08 Sep 2011 10:01

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