DeYoung Brody J, Innes Roger W
Department of Biology, Indiana University, Bloomington, Indiana 47405, USA.
Nat Immunol. 2006 Dec;7(12):1243-9. doi: 10.1038/ni1410.
Plant proteins belonging to the nucleotide-binding site-leucine-rich repeat (NBS-LRR) family are used for pathogen detection. Like the mammalian Nod-LRR protein 'sensors' that detect intracellular conserved pathogen-associated molecular patterns, plant NBS-LRR proteins detect pathogen-associated proteins, most often the effector molecules of pathogens responsible for virulence. Many virulence proteins are detected indirectly by plant NBS-LRR proteins from modifications the virulence proteins inflict on host target proteins. However, some NBS-LRR proteins directly bind pathogen proteins. Association with either a modified host protein or a pathogen protein leads to conformational changes in the amino-terminal and LRR domains of plant NBS-LRR proteins. Such conformational alterations are thought to promote the exchange of ADP for ATP by the NBS domain, which activates 'downstream' signaling, by an unknown mechanism, leading to pathogen resistance.
属于核苷酸结合位点富含亮氨酸重复序列(NBS-LRR)家族的植物蛋白用于病原体检测。就像检测细胞内保守病原体相关分子模式的哺乳动物Nod-LRR蛋白“传感器”一样,植物NBS-LRR蛋白检测病原体相关蛋白,最常见的是负责毒力的病原体效应分子。许多毒力蛋白是植物NBS-LRR蛋白通过毒力蛋白对宿主靶蛋白造成的修饰间接检测到的。然而,一些NBS-LRR蛋白直接结合病原体蛋白。与修饰的宿主蛋白或病原体蛋白结合会导致植物NBS-LRR蛋白的氨基末端和LRR结构域发生构象变化。这种构象改变被认为通过未知机制促进NBS结构域将ADP交换为ATP,从而激活“下游”信号传导,导致病原体抗性。