TaARPC5 is required for wheat defense signaling in response to infection by the stripe rust fungus
TaARPC5 is required for wheat defense signaling in response to infection by the stripe rust fungus
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DOI:
10.1016/j.cj.2021.01.009
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发表时间:
2021-04
期刊:
影响因子:
6.6
通讯作者:
Jia Guo;Huan Peng;Tuo Qi;Sanding Xu;Md Ashraful Islam;B. Day;Qing Ma;Z. Kang;Jun Guo
中科院分区:
文献类型:
--
作者:
Jia Guo;Huan Peng;Tuo Qi;Sanding Xu;Md Ashraful Islam;B. Day;Qing Ma;Z. Kang;Jun Guo
Numerous studies using a combination of confocal microscopic- and pharmacological-based approaches have demonstrated that the actin cytoskeleton dynamically responds to pathogen infection. Here, we observed that phalloidin treatment induced actin nucleation, resulting in enhanced resistance of wheat against the stripe rust pathogenPuccinia striiformisf. sp.tritici(Pst). To define the mechanism underpinning this process, we characterized a family of conserved actin-binding proteins, the actin related protein (ARP) family, which controls actin polymerization. Specifically, we identified and characterized a wheat ARPC gene (TaARPC5), which encodes a 136-amino acid protein containing a P16-Arc domain, the smallest subunit of the ARP2/3 complex.TaARPC5mRNA accumulation was induced following the infection of plants with the avirulentPststrain, and following the elicitation with flagellin (e.g., flg22) as well. Subcellular localization analysis revealed that TaARPC5 is primarily localized to the cortical actin cytoskeleton, and its precise cellular localizations suggest the proximity to processes correlated with the actin-organelle interface. Upon treatment with virulentPst,TaARPC5-knockdown plants exhibited a significant reduction in the expression of PTI-specific mRNAs. Conversely, we observed enhanced induction of reactive oxygen species (ROS) accumulation and a decrease inTaCAT1expression following infection with an incompatiblePstisolate. Together with yeast complementation assays, the current study demonstrates a role forTaARPC5in resistance signaling in wheat againstPstinfection by regulating the host actin cytoskeleton.