Abstract：
:The Arabidopsis immune receptors RPS4 and RRS1 interact to co-confer responsiveness to bacterial effectors. The RRS1-R allele, with RPS4, responds to AvrRps4 and PopP2, whereas RRS1-S responds only to AvrRps4. Here, we show that the C terminus of RRS1-R but not RRS1-S is phosphorylated. Phosphorylation at Thr1214 in the WRKY domain maintains RRS1-R in its inactive state and also inhibits acetylation of RRS1-R by PopP2. PopP2 in turn catalyzes O-acetylation at the same site, thereby preventing its phosphorylation. Phosphorylation at other sites is required for PopP2 but not AvrRps4 responsiveness and facilitates the interaction of RRS1's C terminus with its TIR domain. Derepression of RRS1-R or RRS1-S involves effector-triggered proximity between their TIR domain and C termini. This effector-promoted interaction between these domains relieves inhibition of TIRRPS4 by TIRRRS1. Our data reveal effector-triggered and phosphorylation-regulated conformational changes within RRS1 that results in distinct modes of derepression of the complex by PopP2 and AvrRps4.
journal_name
Cell Host Microbejournal_title
Cell host & microbeauthors
Guo H,Ahn HK,Sklenar J,Huang J,Ma Y,Ding P,Menke FLH,Jones JDGdoi
10.1016/j.chom.2020.03.008subject
Has Abstractpub_date
2020-05-13 00:00:00pages
769-781.e6issue
5eissn
1931-3128issn
1934-6069pii
S1931-3128(20)30172-4journal_volume
27pub_type
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