Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR.

ABSTRACT: Nucleotide-binding leucine-rich repeat (NLR) proteins play a pivotal role in plant immunity by recognizing pathogen effectors^1,2. Maintaining a balanced immune response is crucial, as excessive NLR expression can lead to unintended autoimmunity^3,4. Unlike most NLRs, the plant NLR required for cell death 2 (NRC2) belongs to a small NLR group characterized by constitutively high expression without self-activation⁵. The mechanisms underlying NRC2 autoinhibition and activation are not yet understood. Here we show that Solanum lycopersicum (tomato) NRC2 (SlNRC2) forms dimers and tetramers and higher-order oligomers at elevated concentrations. Cryo-electron microscopy shows an inactive conformation of SlNRC2 in these oligomers. Dimerization and oligomerization no

SUBMITTER: Ma S 

PROVIDER: S-EPMC11338831 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature