Ubiquitin-Like protein 5 interacts with the silencing suppressor p3 of rice stripe virus and mediates its degradation through the 26S proteasome pathway
Ubiquitin-Like protein 5 interacts with the silencing suppressor p3 of rice stripe virus and mediates its degradation through the 26S proteasome pathway
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泛素样蛋白 5 与水稻条纹病毒的沉默抑制子 p3 相互作用，并通过 26S 蛋白酶体途径介导其降解
DOI：
10.1371/journal.ppat.1008780
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发表时间：
2020-08-01
期刊：
影响因子：
6.7
通讯作者：
Yan, Fei
中科院分区：
文献类型：
--
作者：
Chen, Binghua;Lin, Lin;Yan, Fei
泛素样蛋白5（UBL5）与其他蛋白质相互作用以调节其功能，但与泛素和其他UBLs不同，因为它不形成共价缀合物。泛素和大多数UBL通过26S蛋白酶体介导靶蛋白的降解，但尚不清楚UBL 5是否也可以这样做。本研究发现水稻和本氏烟草的UBL5s与水稻条纹病毒（RSV）p3蛋白相互作用。在N.本塞姆氏菌促进RSV感染，而UBL5过表达在两种N.本萨米亚那和大米。进一步的分析表明，NbUBL5.1通过26S蛋白酶体降解p3而损害p3作为沉默抑制子的功能。NbUBL5.1和OsUBL5与26S蛋白酶体中的泛素受体RPN10和RPN13相互作用。此外，NbRPN10或NbRPN13的沉默损害了由NbUBL5.1介导的p3的降解。总之，结果表明，UBL5介导的RSV p3蛋白的降解，通过26 S蛋白酶体，以前未报道的植物防御策略对RSV感染。
Ubiquitin like protein 5 (UBL5) interacts with other proteins to regulate their function but differs from ubiquitin and other UBLs because it does not form covalent conjugates. Ubiquitin and most UBLs mediate the degradation of target proteins through the 26S proteasome but it is not known if UBL5 can also do that. Here we found that the UBL5s of rice and Nicotiana benthamiana interacted with rice stripe virus (RSV) p3 protein. Silencing of NbUBL5s in N. benthamiana facilitated RSV infection, while UBL5 overexpression conferred resistance to RSV in both N. benthamiana and rice. Further analysis showed that NbUBL5.1 impaired the function of p3 as a suppressor of silencing by degrading it through the 26S proteasome. NbUBL5.1 and OsUBL5 interacted with RPN10 and RPN13, the receptors of ubiquitin in the 26S proteasome. Furthermore, silencing of NbRPN10 or NbRPN13 compromised the degradation of p3 mediated by NbUBL5.1. Together, the results suggest that UBL5 mediates the degradation of RSV p3 protein through the 26S proteasome, a previously unreported plant defense strategy against RSV infection.