University of Amsterdam, SILS, Molecular Plant Pathology, Science Park 904, 1098 XH Amsterdam, The Netherlands.
Curr Opin Plant Biol. 2012 Aug;15(4):375-84. doi: 10.1016/j.pbi.2012.05.001. Epub 2012 Jun 1.
Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure-function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure.
许多植物疾病抗性 (R) 蛋白属于核苷酸结合亮氨酸重复 (NB-LRR) 蛋白家族。NB-LRR 介导对病原体衍生效应分子的识别，随后激活宿主防御。它们的多结构域结构允许这些病原体探测器同时充当传感器、开关和反应因子。结构-功能分析和最近对亚结构 3D 结构的阐明，提供了关于这些不同功能如何结合以及各个亚结构的贡献的新见解。除了结构域间的相互作用外，与伴侣蛋白、蛋白酶体和效应诱饵的相互作用对于保持 NB-LRR 在信号转导但自身抑制的状态也是必需的。在这篇综述中，我们基于对其结构的最新理解，探讨了 NB-LRR 功能的操作模型。
