Molecular and functional analysis of a brown planthopper resistance protein with two nucleotide-binding site domains
| Autor: | Bo Du, Lingyun Nie, Rongzhi Chen, Jin Huang, Guangcun He, Lili Zhu, Zhizheng Wang, Qin Guo, Yinxia Hu, Jianping Guo, Ning Zhang |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Hypersensitive response
chemistry.chemical_classification Binding Sites biology Functional analysis Physiology Chemistry Nucleotides Plant Science Plants biology.organism_classification Domain (software engineering) Cell biology Hemiptera Protein Domains Animals Nucleotide Brown planthopper Herbivory Binding site Gene Function (biology) Plant Proteins |
| Zdroj: | Journal of experimental botany. 72(7) |
| ISSN: | 1460-2431 |
| Popis: | The brown planthopper (Nilaparvata lugens Stål, 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. |
| Databáze: | OpenAIRE |
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