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Cell Host Microbe. 2011 Mar 17;9(3):187-199. doi: 10.1016/j.chom.2011.02.008.

Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death.

Author information

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; National Institute of Biological Sciences, Number 7 Science Park Road, Zhongguancun Life Science Park, 102206 Beijing, China.
3
Department of Bioinformatics and Structural Biochemistry, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060036, Bucharest, Romania.
4
Department of Plant Pathology, Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands.
5
National Institute of Biological Sciences, Number 7 Science Park Road, Zhongguancun Life Science Park, 102206 Beijing, China.
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
National Institute of Biological Sciences, Number 7 Science Park Road, Zhongguancun Life Science Park, 102206 Beijing, China; College of Biological Sciences, Tsinghua University, Haidian District, 100084 Beijing, China. Electronic address: chaijijie@nibs.ac.cn.
8
Department of Plant-Microbe Interactions, Max-Planck Institut für Pflanzenzüchtungsforschung, Carl-von-Linne Weg 10, 50829 Cologne, Germany. Electronic address: schlef@mpipz.mpg.de.

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.

PMID:
21402358
DOI:
10.1016/j.chom.2011.02.008
[Indexed for MEDLINE]
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