期刊
CELL HOST & MICROBE
卷 9, 期 3, 页码 187-199出版社
CELL PRESS
DOI: 10.1016/j.chom.2011.02.008
关键词
-
资金
- Max Planck Society
- Deutsche Forschungsgemeinschaft [SFB670]
- European Union [FOOD-CT-2005-513959]
- CNCSIS [249 168/2007]
- Chinese Academy of Sciences [KSCX2-YW-N-075]
- National Outstanding Young Scholar Science Foundation of National Natural Science Foundation of China [20101331722]
- [POSDRU/89/1.5/S/60746]
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据