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《2017中国长三角遗传学大会会议手册》2017年
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Cloning and Mechanism Analysis of CMPG1-V interaction protein ToxABP1-V in Haynaldia villosa

Zongkuan Wangg  Anqi Fang  Zhongyu Yug  Yongli Haog  Jia Zhaog  Heng Zhangg  Haiyan Wangg  Jin Xiaog  Xiue Wang  
【摘要】:The ubiquitin/26 S proteasome system constitutes the major protein degradation pathway in the cell,and plays an important role in various developmental processes of plants,including plant disease resistance.The E3 ligase gene CMPGl-V from Haynaldia villosa,which is rapidly induced by Blumeria graminis tritici(Bgt) inoculation,confers resistance to a broadspectrum of Bgt isolates.To further characterize the mechanism underlying CMPGl-V signaling pathway,we performed yeast two-hybrid(Y2 H) and identified the protein Toxin A Binding protein 1(ToxABPl-V).ToxABPl-V encoded a chloroplast localized protein,and sharply down-regulated after Bgt inoculation in H.villosa.Besides,ToxABP1-V and CMPG1-V exhibite opposite expression profiles after Bgt inoculation.ToxABP1-V physically interacts with the ARM repeat of CMPG1-V in vitro.In addition,CMPG1-V polyubiquitinate ToxABP1-V and promote ToxABP1-V degradation.Transient silencing wheat ToxABP1 s using single-cell transient silencing assay or VIGS enhanced its powdery mildew resistance.Transgenic wheat silencing ToxABP1 s showed improved powdery mildew resistance,associated with an increase in expression of salicylic acid-responsive genes and ROS generating/scavenging genes,H_2 O_2 accumulation,and programmed cell death after Bgt inoculation.These results demonstrate that ToxABP1-V acts as a CMPG1-V substrate,and negatively regulates wheat powdery mildew resistance.

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