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A Disulphide Isomerase Gene(Pdi-V) From Haynaldia Villosa Contributes To Powdery Mildew Resistance In Common Wheat

Muhammad Faheem  Yingbo Li  Muhammad Arshad  Cheng Jiangyue  Zhao Jia  Xiao Jin  Haiyan Wang  Ruiqi Zhang  Liping Xing  Aizhong Cao  Xiue Wang  
【摘要】:In this study, we reported the contribution of PDI-like gene from wheat wild relative Haynaldia villosa in combating against powdery mildew(Bgt). PDI-V was identified by Yeast two hybrid as an interacting protein with CMPG1-V, which encodes an E3 ligase and is a positive regulator for powdery mildew resistance. The PDI-V contains two conserved thioredoxin active domains(a and a′) and an inactive domain(b). Our results showed that PDI-V could be mono-ubiquitinated by CMPG1-V without detected degradation. The PDI-V was located on the 5 V chromosome in H. villosa genome and PDI-V is subcellularly localized in endoplasmic reticulum lumen. PDI-V was induced in leaves when challenged with Bgt. Visible Bgt spores could not be detected when silencing the PDIs in PM resistant T. durum-H. villosa amphiploid, but microscopically display increased fungal growth. Single cell transient over-expression of PDI-V decreased the haustorium index of a moderately PM susceptible wheat variety Yangmai-158. Stable transgenic lines over-expressing PDI-V displayed improved PM resistance at both seedling and adult stages. Over-expression of construct only containing the active thioredoxin domain a could also equally reduce the HI as the full length gene, indicating its critical role in defense responses. Over-expressed point mutated PDI-VC57 Ain Yangmai-158 could not improve PM resistance, further confirming the essential role of the conserved TRX-like domain a for proper functioning of PDI-V. Taken together, these evidences indicates that PDI-V plays positive role in PM resistance and represents a potential novel source for wheat improvement.

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