The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor.

The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor.
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DOI:
10.1111/nph.12418
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发表时间:
2013-11
期刊:
The New phytologist
影响因子:
--
通讯作者:
Yihe Yu;Weirong Xu;Jie Wang;Lei Wang;Wenkong Yao;Ya-zhou Yang;Yan Xu;Fuli Ma;Yangjian Du
Yihe Yu;Weirong Xu;Jie Wang;Lei Wang;Wenkong Yao;Ya-zhou Yang;Yan Xu;Fuli Ma;Yangjian Du
中科院分区:
其他
文献类型:
--
作者:
Yihe Yu;Weirong Xu;Jie Wang;Lei Wang;Wenkong Yao;Ya-zhou Yang;Yan Xu;Fuli Ma;Yangjian Du

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泛素介导的调节对特定刺激快速反应;这种快速对病原体攻击的防御反应特别重要。在这里,我们研究了E3泛素连接酶Erysihe Necator-Induced Ring Finger Protein 1(EIRP1)在中国野生葡萄防御性反应中的作用。用分子、遗传学和生物化学方法研究了E3泛素连接酶EIRP1的调控功能。EIRP1编码一种C3HC4型真正有趣的新基因(环)指蛋白,含有E3连接酶活性。这一活动需要保守的环域,VpWRKY11也通过环域与EIRP1相互作用。VpWRKY11定位于细胞核,激活足底W-box依赖的转录。EIRP1在体内靶向VpWRKY11,导致VpWRKY11降解。EIRP1和VpWRKY11在葡萄白粉病中的表达对白粉病反应迅速;EIRP1在拟南芥中的过表达增强了对病原菌Golovinmyces cichoracearum和Pseudomonas syringae PV番茄DC3000的抗性。我们的数据表明,EIRP1 E3连接酶通过26S蛋白酶体的降解介导负调控因子VpWRKY11的蛋白降解,从而正向调节植物的抗病能力。
Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata. The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4-type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W-box-dependent transcription in planta. EIRP1 targeted VpWRKY11 in vivo, resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome.