TIR‐NB‐LRR immune receptor SOC3 pairs with truncated TIR‐NB protein CHS1 or TN2 to monitor the homeostasis of E3 ligase SAUL1. Issue 4 (10th November 2018)

• Record Type: Journal Article
• Authors: Liang, Wanwan; van Wersch, Solveig; Tong, Meixuezi; Li, Xin
• Is Part Of: New phytologist. Volume 221:Issue 4(2019)
• Page Start: 2054
• Page End: 2066
• Publication Date: 2018-11-10
• Subjects: CHS1 -- E3 ligase -- NLR immune receptor -- paired NLRs -- plant immunity -- SAUL1 -- SOC3 -- TN2; Botany -- Periodicals; 580
• DOI: 10.1111/nph.15534
• Languages: English
• ISSNs: 0028-646X

Abstract

Summary: Intracellular nucleotide binding (NB) and leucine‐rich repeat (NLR) proteins function as immune receptors to recognize effectors from pathogens. They often guard host proteins that are the direct targets of those effectors. Recent findings have revealed that a typical NLR sometimes cooperates with another atypical NLR for effector recognition. Here, by using the CRISPR/Cas9 gene editing method, knockout analysis and biochemical assays, we uncovered differential pairings of typical Toll Interleukin1 receptor (TIR) type NLR (TNL) receptor SOC3 with atypical truncated TIR‐NB (TN) proteins CHS1 or TN2 to guard the homeostasis of the E3 ligase SAUL1. Overaccumulation of SAUL1 is monitored by the SOC3−TN2 pair, while SAUL1's disappearance is guarded by the SOC3−CHS1 pair. SOC3 forms a head‐to‐head genomic arrangement with CHS1 and TN2, indicative of transcriptional co‐regulation. Such intricate cooperative interactions can probably 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.