杀菌剂
琥珀酸脱氢酶
化学
毒性
生物化学
脱氢酶
生物物理学
线粒体
蛋白质亚单位
立体化学
酶
作者
Guoxian Wang,Mei Xue,Jinyu Wang,Zishu Wang,Beixing Li,Li Zhang,Wei Mu,Feng Liu
标识
DOI:10.1021/acs.jafc.5c15458
摘要
Genetic differentiation of the succinate dehydrogenase (SDH) subunit C in Fusarium spp. contributes to significant variations in the efficacy of succinate dehydrogenase inhibitor (SDHI) fungicides against these pathogens. However, the structural states of the two SDH conformations in mitochondria and their binding modes with SDHI fungicides are still unknown. Based on SDH activity and qRT-PCR assay, we confirmed that the SDH of “C2” conformation in Fusarium pseudograminearum is a constitutively expressed type, while that of “C1” conformation is an inducibly expressed type.Through molecular docking, the difference in binding affinity between SDHI fungicides and the two conformations also proves to be a key factor contributing to the variations in toxicity of SDHI fungicides against F. pseudograminearum. These results established that SDHI fungicides induce the expression of SDH of “C1” conformation, which leads to weak binding between SDHI fungicides and the target, thereby resulting in variations in the toxicity of SDHI fungicides.
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