Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death |
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| Authors: | Maekawa Takaki Cheng Wei Spiridon Laurentiu N Töller Armin Lukasik Ewa Saijo Yusuke Liu Peiyuan Shen Qian-Hua Micluta Marius A Somssich Imre E Takken Frank L W Petrescu Andrei-Jose Chai Jijie Schulze-Lefert Paul |
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| Affiliation: | 1. Department of Plant-Microbe Interactions, Max-Planck Institut für Pflanzenzüchtungsforschung, Carl-von-Linne Weg 10, 50829 Cologne, Germany;2. Beijing Normal University, Haidian District, 19 Xinjiekouwai Street, 100875 Beijing, China;3. National Institute of Biological Sciences, Number 7 Science Park Road, Zhongguancun Life Science Park, 102206 Beijing, China;4. Department of Bioinformatics and Structural Biochemistry, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060036, Bucharest, Romania;5. Department of Plant Pathology, Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands;6. State Key Laboratory of Plant Cell and Chromosome Engineering, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Datun Road, Chaoyang District, 100101 Beijing, China;7. College of Biological Sciences, Tsinghua University, Haidian District, 100084 Beijing, China |
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| Abstract: | Plants and animals have evolved structurally related innate immune sensors, designated NLRs, to detect intracellular nonself molecules. NLRs are modular, consisting of N-terminal coiled-coil (CC) or TOLL/interleukin-1 receptor (TIR) domains, a central nucleotide-binding (NB) domain, and C-terminal leucine-rich repeats (LRRs). The polymorphic barley mildew A (MLA) locus encodes CC-containing allelic immune receptors recognizing effectors of the pathogenic powdery mildew fungus. We report the crystal structure of an MLA receptor's invariant CC domain, which reveals a rod-shaped homodimer. MLA receptors also self-associate in?vivo, but self-association appears to be independent of effector-triggered receptor activation. MLA CC mutants that fail to self-interact impair in planta cell death activity triggered by the CC domain alone and by an autoactive full-length MLA receptor that mimics its ATP-bound state. Thus, CC domain-dependent dimerization of the immune sensor defines a minimal functional unit and implies a role for the dimeric CC module in downstream immune signaling. |
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