4.2 Article

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

Journal

PROTEIN EXPRESSION AND PURIFICATION
Volume 72, Issue 2, Pages 169-174

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2010.03.018

Keywords

Oryza sativa constitutive disease resistance 1 (OsCDR1); Aspartic proteinase (AP); Salicylic acid (SA); Pathogenesis-related (PR) gene; Glutathione-S-transferase (GST)

Funding

  1. UK Biotechnology and Biological Sciences Research Council
  2. Department of Biotechnology, Ministry of Science and Technology, Government of India
  3. UK Government Global Opportunities Fund

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The Oryza saliva 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. (C) 2010 Elsevier Inc. All rights reserved.

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