The Ubiquitin E3 Ligase PUB17 Positively Regulates Immunity by Targeting a Negative Regulator, KH17, for Degradation
作者机构：Division of Plant ScienceSchool of Life ScienceUniversity of Dundee(at JHI)InvergowrieDundee DD25DAUK Key Laboratory of Horticultural Plant Biology(HZAU)Ministry of EducationKey Laboratory of Potato Biology and Biotechnology(HZAU)Ministry of Agriculture and Rural AffairsHuazhong Agricultural UniversityWuhanHubei 430070China Cell and Molecular ScienceJames Hutton InstituteInvergowrieDundee DD25DAUK
出 版 物：《Plant Communications》 (植物通讯（英文）)
年 卷 期：2020年第1卷第4期
页 面：75-86页
核心收录：
基 金：support from the Biotechnology and Biological Sciences Research Council(BBSRC)grants BB/P020569/1,BB/N009967/1,and BB/L026880/1 the Scottish Government Rural and Environment Science and Analytical Services Division(RESAS) supported by funding from The National Natural Science Foundation of China(grants 31761143007,31471550)
主 题：oomycete plant disease late blight E3 ligase KH RNA-binding protein
摘 要：Ubiquitination is a post-translational modification that regulates many processes in *** ubiquitin E3 ligases act as either positive or negative regulators of immunity by promoting the degradation of different ***17 is an E3 ligase that has previously been shown to positively regulate immunity to bacteria,fungi and oomycetes,including the late blight pathogen Phytophthora *** of StPUB17 promotes pathogen colonization and attenuates Cf4/avr4 cell *** yeast-2-hybrid and co-immunoprecipitation we identified the putative K-homology(KH)RNA-binding protein(RBP),StKH17,as a candidate substrate for degradation by ***17 acts as a negative regulator of immunity that promotes *** infection and suppresses specific immune pathways.A KH RBP domain mutant of StKH17(StKH17GDDG)is no longer able to negatively regulate immunity,indicating that RNA binding is likely required for StKH17 *** StPUB17 is a known target of the ubiquitin E3 ligase,StPOB1,we reveal an additional step in an E3 ligase regulatory cascade that controls plant defense.
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