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- Title
Plant NLR immune receptor Tm-2<sup>2</sup> activation requires NB-ARC domain-mediated self-association of CC domain.
- Authors
Wang, Junzhu; Chen, Tianyuan; Han, Meng; Qian, Lichao; Li, Jinlin; Wu, Ming; Han, Ting; Cao, Jidong; Nagalakshmi, Ugrappa; Rathjen, John P.; Hong, Yiguo; Liu, Yule
- Abstract
The nucleotide-binding, leucine-rich repeat-containing (NLR) class of immune receptors of plants and animals recognize pathogen-encoded proteins and trigger host defenses. Although animal NLRs form oligomers upon pathogen recognition to activate downstream signaling, the mechanisms of plant NLR activation remain largely elusive. Tm-22 is a plasma membrane (PM)-localized coiled coil (CC)-type NLR and confers resistance to Tobacco mosaic virus (TMV) by recognizing its viral movement protein (MP). In this study, we found that Tm-22 self-associates upon recognition of MP. The CC domain of Tm-22 is the signaling domain and its function requires PM localization and self-association. The nucleotide-binding (NB-ARC) domain is important for Tm-22 self-interaction and regulates activation of the CC domain through its nucleotide-binding and self-association. (d)ATP binding may alter the NB-ARC conformation to release its suppression of Tm-22 CC domain-mediated cell death. Our findings provide the first example of signaling domain for PM-localized NLR and insight into PM-localized NLR activation. Author summary: Nucleotide-binding, leucine-rich repeat proteins (NLR) can function as immune receptors of plants and animals and confer resistance against pathogens. However, despite their importance in immunity, the activation mechanism of PM-localized NLRs remains largely elusive. In this study, we demonstrate that CC domain is the signaling domain for inducing cell death for PM-localized NLR Tm-22. Further, we report that nucleotide-binding (NB-ARC) domain is important for Tm-22 self-association and regulates activation of CC domain through its nucleotide-binding and self-association. Our findings provide the first example of signaling domain for PM-localized NLR and insight into PM-localized NLR activation.
- Subjects
TOBACCO mosaic virus; PLANT capacity; VIRAL proteins; CELL membranes; CELL death
- Publication
PLoS Pathogens, 2020, Vol 16, Issue 4, p1
- ISSN
1553-7366
- Publication type
Article
- DOI
10.1371/journal.ppat.1008475