Journal Article

Fumarylacetoacetate hydrolase targeted by a Fusarium graminearum effector positively regulates wheat FHB resistance

Li, Hanqi, Fan, Yujin, Zhou, Xishi, Xing, Xiaoping, Hu, Qianyong, Wang, Yiwei, He, Yuhan, Zhao, Ruihua, Fang, Ying, Wang, Penghao, Shang, Shengping, Zhang, Cui-Jun

2025

Overview

Fusarium head blight (FHB), caused by Fusarium graminearum is a devastating disease that affects global wheat production. F. graminearum encodes many effector proteins; however, its virulence mechanisms are poorly understood. In this study, we identify a secretory e ffector c andidate (FgEC10) that is essential for the virulence of F. graminearum . FgEC10 interacts strongly with wheat fumarylacetoacetate hydrolase (TaFAH) and accelerates its degradation via the 26S proteasome pathway. In addition, we show that TaFAH interacts with proteasome 26S subunit, non-ATPases 12 (TaPSMD12) and that FgEC10 enhances the interaction between TaFAH and TaPSMD12. RNA silencing or overexpression of TaFAH in wheat plants shows that TaFAH positively regulates wheat FHB resistance. Overexpression of TaFAH promotes the expression of genes associated with disease resistance and the heading period. Metabolomic analysis reveals that overexpression of TaFAH increases the levels of several amino acids in wheat, and exogenous application of some of these amino acids show an increase in F. graminearum resistance in the wheat spike and seedling. Collectively, our study reveals a pathogenic mechanism and provides a valuable gene resource for improving FHB resistance and promoting heading in wheat. A Fusarium graminearum effector is found to target wheat fumarylacetoacetate hydrolase for 26S proteasomal degradation. The hydrolase enhances resistance to Fusarium head blight by regulating defense genes and amino acid metabolism, offering a genetic target for wheat improvement.

• Publisher: Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
• Subject: 13/89 / 14/19 / 14/35 / 38/77 / 38/88 / 631/326/193/2542 / 631/449/2169/2673 / 631/449/2169/597 / 82/1 / 82/83 / Amino acids / Binding sites / Biosynthesis / Blight / Crop production / Degradation / Disease resistance / Enzymes / Fumarylacetoacetase / Fusarium / Fusarium - genetics / Fusarium - pathogenicity / Fusarium - physiology / Fusarium graminearum / Fusarium head blight / Genes / Genetic resources / Humanities and Social Sciences / Hydrolase / Hydrolases - metabolism / Infections / Kinases / Metabolomics / Morphology / multidisciplinary / Pathogens / Plant Diseases - immunology / Plant Diseases - microbiology / Plant Proteins - metabolism / Proteasome 26S / Proteasome Endopeptidase Complex - metabolism / Proteasomes / Proteins / RNA-mediated interference / Science / Science (multidisciplinary) / Seedlings / Triticum - enzymology / Triticum - immunology / Triticum - microbiology / Virulence / Wheat