Abstract:
: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 NBS (Nuceotide binding site) domains. To understand how this CC-NBS-NBS-LRR 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 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 LRR domains of BPH9 associate with each other and themselves in planta. Further domain swapping experiments revealed the CC domains of BPH9 and susceptible alleles were similarly competent to induce resistance and HR (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.
journal_name
J Exp Botjournal_title
Journal of experimental botanyauthors
Wang Z,Huang J,Nie L,Hu Y,Zhang N,Guo Q,Guo J,Du B,Zhu L,He G,Chen Rdoi
10.1093/jxb/eraa586subject
Has Abstractpub_date
2020-12-21 00:00:00eissn
0022-0957issn
1460-2431pii
6042569pub_type
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