Solveig van Wersch / University of British Columbia
Xin Li / University of British Columbia
Meixuezi Tong / University of British Columbia
Intracellular NB-LRR proteins (NLRs) function as immune receptors to recognize effectors from pathogens. They often guard host proteins that are the direct targets of those effectors. Recent findings revealed that a typical NLR sometimes cooperates with another atypical NLR for effector recognition.
Here, by using CRISPR-Cas9 genome-editing technology, genetic analysis and biochemical assays, we report on the differential pairings of TNL receptor SOC3 with TN proteins CHS1 or TN2 to guard the homeostasis of the E3 ligase SAUL1.
SAUL1 over-accumulation is monitored by SOC3-TN2 and SAUL1’s disappearance is guarded by SOC3-CHS1. SOC3 forms a head-to-head genomic arrangement with CHS1 and TN2, indicative of transcriptional co-regulation.
Such cooperative interactions can likely enlarge the recognition spectrum and increase the functional flexibility of NLRs, which can partly explain the overwhelming occurrence of NLR gene clustering in higher plants.