Submitted to: Plant and Animal Genome Conference Proceedings
Publication Type: Proceedings
Publication Acceptance Date: 1/1/2006
Publication Date: 2/15/2006
Citation: Lee, J., Bricker, T.M., Lebevre, M., Pinson, S.R., Cooper, B., Oard, J.H. 2006. Complementary proteomic and genetic analyses of rice response to challenge by the fungal pathogen Rhizoctonia solani [abstract]. Plant and Animal Genome Conference Proceedings. p. P253.
Technical Abstract: Rice (Oryza sativa L.) is considered a model crop plant due to its importance worldwide as a food source, a small diploid genome suitable for genetic and proteomic analyses, and completion of the rice genome sequence. The objective of our research was to utilize both proteomic and genetic approaches that would complement and enhance our outstanding of rice sheath blight disease caused by R. solani, a fungal pathogen of worldwide importance to not only rice, but to many other important crops in the world as well. For our proteomic study, we identified 14 up-regulated proteins via 2D-PAGE and ESI Q-TOF MS methods in a rice resistant mutant after challenge by R. solani. The proteins were identified with presumed functions relating to antifungal activity, signal transduction, energy metabolism, photosynthesis, protein folding, proteolysis, and antioxidation. The induction of 3-B-hydroxysteroid dehydrogenase/isomerase was detected for the first time in rice, suggesting a defensive role of this enzyme against attack by R. solani. For the genetic component, we identified 15 QTL regions on a genetic map for resistance to sheath blight in a large rice breeding population evaluated under field conditions. The upregulated proteins were found to map within the QTL regions of the breeding population which suggest that the identified proteins have functional roles in response to stress imposed by R. solani. These studies demonstrate that complementary proteomic and genetic approaches can effectively enhance our ability to identify candidate genes for disease resistance and their corresponding proteins for basic and applied research.