Title: | Molecular and functional analysis of a brown planthopper resistance protein with two nucleotide-binding site domains |
Author(s): | Wang Z; Huang J; Nie L; Hu Y; Zhang N; Guo Q; Guo J; Du B; Zhu L; He G; Chen R; |
Address: | "State Key Laboratory of Hybrid Rice, College of Life Sciences, Wuhan University, Wuhan, China" |
ISSN/ISBN: | 1460-2431 (Electronic) 0022-0957 (Linking) |
Abstract: | "The brown planthopper (Nilaparvata lugens Stal, BPH) resistance gene BPH9 encodes an unusual coiled-coil (CC) nucleotide-binding leucine-rich repeat (LRR) protein with two nucleotide-binding site (NBS) domains. To understand how this CC-NBS-NBS-LRR (CNNL) protein regulates defense signaling and BPH resistance, we dissected each domain's functions. The CC domain of BPH9 self-associated and was sufficient to induce cell death. The region of 97-115 residues in the CC domain is crucial for self-association and activation. NBS2, which contains a complete set of NBS function motifs and inhibits CC domain activation, rather than NBS1, acts as a molecular switch to regulate the activity of BPH9. We demonstrated that the CC domain, the NBS domain, and the LRR domain of BPH9 associate with each other and themselves in planta. Further domain swapping experiments revealed that the CC domains of BPH9 and susceptible alleles were similarly competent to induce resistance and the hypersensitive response, while the LRR domain of BPH9 confers resistance specificity to BPH. These findings provide new insights into the regulatory mechanisms governing the activity of CNNL proteins" |
Keywords: | Animals Binding Sites *Hemiptera Herbivory Nucleotides *Plant Proteins/genetics/metabolism Plants/*genetics Protein Domains Brown planthopper (BPH) coiled-coil (CC) hypersensitivity response (HR) insect-plant interaction nucleotide-binding leucine-rich re; |
Notes: | "MedlineWang, Zhizheng Huang, Jin Nie, Lingyun Hu, Yinxia Zhang, Ning Guo, Qin Guo, Jianping Du, Bo Zhu, Lili He, Guangcun Chen, Rongzhi eng Research Support, Non-U.S. Gov't England 2020/12/22 J Exp Bot. 2021 Mar 29; 72(7):2657-2671. doi: 10.1093/jxb/eraa586" |