TaADF4, an actin‐depolymerizing factor from wheat, is required for resistance to the stripe rust pathogen Puccinia striiformis f. sp. tritici

• DOI: 10.1111/tpj.13459
• Publication Date: 2016-12-20T07:06:37Z
• Authors: Bing Zhang; Yuan Hua; Juan Wang; Yan Huo; Masaki Shimono; Brad Day; Qing Ma
• Keywords: Jasmonic acid

Actin filament assembly in plants is a dynamic process, requiring the activity of more than 75 actin-binding proteins. Central to regulation and stability conserved family actin-depolymerizing factors (ADFs), whose primarily function regulate severing depolymerization actin filaments. In recent years, ADF proteins has been linked variety cellular processes, including those associated with response stress. Herein, wheat gene, TaADF4, was identified characterized. TaADF4 encodes 139-amino-acid protein containing five F-actin-binding sites two G-actin-binding sites, interacts (Triticum aestivum) Actin1 (TaACT1), planta. Following treatment wheat, separately, jasmonic acid, abscisic acid or avirulent race, CYR23, stripe rust pathogen Puccinia striiformis f. sp. tritici, we observed rapid induction accumulation mRNA. Interestingly, mRNA diminished inoculation virulent CYR31. Silencing resulted enhanced susceptibility demonstrating role for defense signaling. Using pharmacological-based approach, coupled an analysis host infection, that actin-modifying agent latrunculin B resistance increased production reactive oxygen species enhancement localized hypersensitive cell death. Taken together, these data support hypothesis positively modulates plant immunity via modulation cytoskeletal organization.