Structual analysis of R protein activation

2016 Fiscal Year Final Research Report

• Project/Area Number: 26450055
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Plant protection science
• Research Institution: Yokohama City University (2016); Nara Institute of Science and Technology (2014-2015)
• Principal Investigator: Kawano Yoji 横浜市立大学, 木原生物学研究所, 客員准教授 (00406175)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: イネ / R タンパク質

Outline of Final Research Achievements

Although resistant (R) proteins are important intracellular immune receptors that induce the strongest immune response in plants, it is difficult to purify full-length R proteins, so signal transduction and activation mechanisms of R proteins remain largely unclear. We have previously reported that rice R protein Pit confers resistance to rice blast fungus and plays important roles in rice innate immunity. However, it is largely unknown how Pit induces downstream immune responses. In this study, we performed the biochemical analyses using purified the CC domain and the NB-ARC domain of Pit recombinant proteins to clarify activation mechanisms of Pit-1. We found that the exchange of ADP/ATP binding in the NB-ARC domain of Pit influences the intramolecular interaction between the CC domain and the NB-ARC domain of Pit. Moreover, we demonstrated here that the CC domain of Pit forms a dimer and a super oligomer in solution.

Free Research Field

植物生物学