Open AccessPerception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor
Author(s) -
Nitika Mukhi,
Hannah Brown,
Danylo Gorenkin,
Pingtao Ding,
Adam R. Bentham,
Clare E. M. Stevenson,
Jonathan D. G. Jones,
Mark J. Banfield
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2113996118
Subject(s) - effector , wrky protein domain , arabidopsis , biology , pseudomonas syringae , immune receptor , virulence , immune system , microbiology and biotechnology , computational biology , genetics , pathogen , gene , mutant
Significance This study reveals a mechanism for effector perception by a plant NLR immune receptor that contains an integrated domain (ID) that mimics an authentic effector target. TheArabidopsis immune receptors RRS1 and RPS4 detect thePseudomonas syringae pv.pisi secreted effector AvrRps4 via a WRKY ID in RRS1. We used structural biology to reveal the mechanisms of AvrRps4C –WRKY interaction and demonstrated that this binding is essential for effector recognition in planta. Our analysis revealed features of the WRKY ID that mediate perception of structurally distinct effectors from different bacterial pathogens. These insights could enable engineering NLRs with novel recognition specificities, and enhance our understanding of how effectors interact with host proteins to promote virulence.