Department of Biology, Indiana University, Bloomington, Indiana 47405, USA; email:
Annu Rev Phytopathol. 2020 Aug 25;58:139-160. doi: 10.1146/annurev-phyto-010820-012733. Epub 2020 Apr 13.
Focusing on the discovery and characterization of the disease resistance protein RPS5 and its guardee PBS1, this review discusses work done in the Innes laboratory from the initial identification of the gene in 1995 to the recent deployment of the PBS1 decoy system in crops. This is done through discussion of the structure, function, and signaling environment of RPS5 and PBS1, highlighting collaborations and influential ideas along the way. RPS5, a nucleotide-binding leucine-rich repeat (NLR) protein, is activated by the proteolytic cleavage of PBS1. We have shown that the cleavage site within PBS1 can be altered to contain cleavage sites for other proteases, enabling RPS5 activation by these proteases, thereby conferring resistance to different pathogens. This decoy approach has since been translated into crop species using endogenous PBS1 orthologs and holds strong potential for GMO-free development of new genetic resistance against important crop pathogens.
本文聚焦于疾病抗性蛋白 RPS5 和其保护蛋白 PBS1 的发现和特性描述。该综述讨论了 Innes 实验室从 1995 年最初鉴定该基因到最近在作物中应用 PBS1 诱饵系统的工作。文中通过讨论 RPS5 和 PBS1 的结构、功能和信号环境，突出了沿途的合作和有影响力的想法。RPS5 是一种核苷酸结合亮氨酸重复（NLR）蛋白，其活性受 PBS1 的蛋白水解切割调控。我们已经证明，PBS1 中的切割位点可以被改变以包含其他蛋白酶的切割位点，从而使这些蛋白酶能够激活 RPS5，从而赋予对不同病原体的抗性。此后，该诱饵方法已被应用于使用内源性 PBS1 同源物的作物物种，并为开发针对重要作物病原体的新型遗传抗性而无需使用转基因生物提供了巨大潜力。
