The Sw-5b NLR nucleotide-binding domain plays a role in oligomerization, and its self-association is important for activation of cell death signaling

突变体 细胞生物学 生物 程序性细胞死亡 信号转导 细胞信号 受体 遗传学 细胞凋亡 基因
作者
Xiaohui Zhao,Zhengqiang Chen,Qian Wu,Yazhen Cai,Yu Zhang,Ruizhen Zhao,Jiaoling Yan,Xin Qian,Jia Li,Min Zhu,Lizhou Hong,Jincheng Xing,Nasr Ullah Khan,Yinghua Ji,Peijun Wu,Changjun Huang,Xin Shun Ding,Hui Zhang,Xiaorong Tao
出处
期刊:Journal of Experimental Botany [Oxford University Press]
卷期号:72 (18): 6581-6595 被引量:6
标识
DOI:10.1093/jxb/erab279
摘要

Plant and animal intracellular nucleotide-binding and leucine-rich repeat (NLR) receptors play important roles in sensing pathogens and activating defense signaling. However, the molecular mechanisms underlying the activation of host defense signaling by NLR proteins remain largely unknown. Many studies have determined that the coil-coil (CC) or Toll and interleukin-1 receptor/resistance protein (TIR) domain of NLR proteins and their dimerization/oligomerization are critical for activating downstream defense signaling. In this study, we demonstrated that, in tomato, the nucleotide-binding (NB) domain Sw-5b NLR alone can activate downstream defense signaling, leading to elicitor-independent cell death. Sw-5b NB domains can self-associate, and this self-association is crucial for activating cell death signaling. The self-association was strongly compromised after the introduction of a K568R mutation into the P-loop of the NB domain. Consequently, the NBK568R mutant induced cell death very weakly. The NBCΔ20 mutant lacking the C-terminal 20 amino acids can self-associate but cannot activate cell death signaling. The NBCΔ20 mutant also interfered with wild-type NB domain self-association, leading to compromised cell death induction. By contrast, the NBK568R mutant did not interfere with wild-type NB domain self-association and its ability to induce cell death. Structural modeling of Sw-5b suggests that NB domains associate with one another and likely participate in oligomerization. As Sw-5b-triggered cell death is dependent on helper NLR proteins, we propose that the Sw-5b NB domain acts as a nucleation point for the assembly of an oligomeric resistosome, probably by recruiting downstream helper partners, to trigger defense signaling.

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