J Integr Plant Biol ›› 2025, Vol. 67 ›› Issue (11): 3032-3050.DOI: 10.1111/jipb.70023

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  • 收稿日期:2025-01-26 接受日期:2025-07-26 出版日期:2025-11-01 发布日期:2025-11-08

Histone deacetylase MiHDA3 enhances mango fruit resistance to Colletotrichum gloeosporioides by deacetylating MiCAT1

Yue Xiang1, Donald J. Huber2, Lisha Zhu1, Xuewu Duan3, Xiangbin Xu1, Yueming Jiang3, Guoxiang Jiang3*, Zhengke Zhang1*    

  1. 1. School of Food Science and Engineering, Hainan University, Haikou 570228, China
    2. Horticultural Sciences Department, University of Florida, Gainesville, FL 32611‐0690, USA
    3. Guangdong Provincial Key Laboratory of Applied Botany & State Key Laboratory of Plant Diversity and Specialty Crops, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, China

    *Correspondences: Guoxiang Jiang (gxjiang@scbg.ac.cn); Zhengke Zhang (zhangzhengke@hainanu.edu.cn, Dr. Zhang is fully responsible for the distribution of all materials associated with this article)
  • Received:2025-01-26 Accepted:2025-07-26 Online:2025-11-01 Published:2025-11-08
  • Supported by:
    This study was financially supported by the Natural Science Foundation of Hainan Province, China (Grant No. 324RC456), National Natural Science Foundation of China (Grant No.32460786), South China Botanical Garden, Chinese Academy of Sciences (Grant No. QNXM‐202306), the Guangdong Science and Technology Plan Project (Grant No. 2023B1212060046), and the Foundation of Key Laboratory of South China Agricultural Plant Molecular Analysis and Genetic Improvement, South China Botanical Garden, Chinese Academy of Sciences (Guangzhou, China).

Abstract: The anthracnose caused by Colletotrichum gloeosporioides poses a significant threat to the global mango (Mangifera indica L.) fruit industry. Although histone deacetylases (HDACs) are well recognized to be involved in plant immunity, the role of HDAC-mediated nonhistone deacetylation in the fruit immune response remains elusive. In the present study, MiHDA3, an HDAC from the RPD3/HDA1 subfamily, was identified as a candidate for regulating mango resistance based on the greatest induction of MiHDA3 in response to infection of C. gloeosporioides among the 19 tested HDAC genes. Transient overexpression of MiHDA3 in mango fruit strengthened the disease resistance by enhancing the activities of defense-related enzymes (phenylalanine ammonia-lyase (PAL) and β-1,3-glucanase (GLU)) and upregulating the expression levels of MiPAL and MiGLU. These increases occurred concomitantly with increased accumulation of local H2O2, a critical signaling molecule. The opposite effects on resistance and H2O2 production were observed in MiHDA3-silenced mango fruit. Physiological assays revealed that exogenous H2O2 treatment suppressed anthracnose development in mango fruit after inoculation with C. gloeosporioides, whereas treatment with diphenylene iodonium, an inhibitor of endogenous H2O2 generation, exacerbated disease symptoms. Furthermore, the mango catalase 1 (MiCAT1), a redox homeostasis-related protein, was confirmed to negatively regulate the resistance of mango fruit to C. gloeosporioides by catalyzing the decomposition of H2O2. Mechanistic investigations revealed that MiHDA3-mediated deacetylation of MiCAT1 at lysine residues K227 and K233 reduced the enzymatic activity and protein stability of MiCAT1, contributing to enhanced resistance in mango fruit. Collectively, these findings highlight that the functional interplay between HDACs and catalases can modulate the immune response in post-harvest fruits, and reveal a novel mechanism by which HDACs enhance mango disease resistance through the deacetylation of nonhistone proteins and the regulation of their biochemical functions.

Key words: catalase, histone deacetylase, immune response, mango anthracnose, nonhistone deacetylation

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