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.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Wang J,Chen T,Han M,Qian L,Li J,Wu M,Han T,Cao J,Nagalakshmi U,Rathjen JP,Hong Y,Liu Ydoi
10.1371/journal.ppat.1008475subject
Has Abstractpub_date
2020-04-27 00:00:00pages
e1008475issue
4eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-20-00025journal_volume
16pub_type
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