Shirasu Ken, Schulze-Lefert Paul
The Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich, UK NR4 7UH.
Trends Plant Sci. 2003 Jun;8(6):252-8. doi: 10.1016/S1360-1385(03)00104-3.
Accumulating evidence indicates that plant disease-resistance (R) proteins assemble in hetero-multimeric protein complexes in the absence of pathogens. Such complexes might enable the indirect recognition of pathogen effector molecules during attempted pathogen invasion. RAR1 and SGT1 are required for the function of most known R proteins. They interact with each other and with diverse protein complexes, which might explain their multi-functionality. The promiscuous behavior of RAR1 and SGT1 might be crucial for the formation and activation of R protein-containing recognition complexes as well as for regulating downstream signaling processes.
越来越多的证据表明，植物抗病（R）蛋白在没有病原体的情况下组装成异源多聚体蛋白复合物。在病原体试图入侵期间，这种复合物可能有助于间接识别病原体效应分子。大多数已知的R蛋白的功能都需要RAR1和SGT1。它们相互作用，并与多种蛋白复合物相互作用，这可能解释了它们的多功能性。RAR1和SGT1的混杂行为对于含R蛋白的识别复合物的形成和激活以及调节下游信号传导过程可能至关重要。
