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<p>Plants require the activation of thermotolerance-related signaling pathways to cope with heat stress, and it is well established that epigenetic regulation plays a critical role in this activation. The plant-specific deacetylase HD2C has been shown to regulate various environmental stress-responsive genes, including those involved in the adaptation of plants to heat stress. Previous research has indicated that HOS15, acting as a substrate receptor of the CUL4-based ubiquitin E3 ligase complex, degrades Histone Deacetylase 2C (HD2C), thus epigenetically activating target cold-responsive genes. However, the mechanism by which HOS15 regulates heat-responsive genes at the chromatin level remains to be elucidated. Here, we report that loss of function of HOS15 mutant plants show sensitivity to heat stress. Our qPCR data show that the expression pattern of <i>Heat Shock Factor A3 (HsfA3)</i> and <i>Heat Shock Protein 101 (HSP101)</i> were downregulated in <i>hos15</i> mutant compared to wild type in response to heat stress. Interestingly, HOS15 and HD2C protein levels remain declined during heat stress whereas, HD2C protein was accumulated in <i>hos15</i> mutants. These results suggest that HOS15 affects the HD2C stabilization different from cold stress during heat stress which positively regulates heat responsive genes such as <i>HsfA3</i>, <i>HSP101</i>.</p>

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HOS15 Contributes to Thermotolerance Through Destabilization of HD2C in Arabidopsis

  • 期刊论文

  • 发表日期：

    2025年6月6日

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  • Kisuk Park,
  • Chae Jin Lim,
  • Nassem Albakri,
  • Min Jae Bae,
  • Junghoon Park

摘要

Plants require the activation of thermotolerance-related signaling pathways to cope with heat stress, and it is well established that epigenetic regulation plays a critical role in this activation. The plant-specific deacetylase HD2C has been shown to regulate various environmental stress-responsive genes, including those involved in the adaptation of plants to heat stress. Previous research has indicated that HOS15, acting as a substrate receptor of the CUL4-based ubiquitin E3 ligase complex, degrades Histone Deacetylase 2C (HD2C), thus epigenetically activating target cold-responsive genes. However, the mechanism by which HOS15 regulates heat-responsive genes at the chromatin level remains to be elucidated. Here, we report that loss of function of HOS15 mutant plants show sensitivity to heat stress. Our qPCR data show that the expression pattern of Heat Shock Factor A3 (HsfA3) and Heat Shock Protein 101 (HSP101) were downregulated in hos15 mutant compared to wild type in response to heat stress. Interestingly, HOS15 and HD2C protein levels remain declined during heat stress whereas, HD2C protein was accumulated in hos15 mutants. These results suggest that HOS15 affects the HD2C stabilization different from cold stress during heat stress which positively regulates heat responsive genes such as HsfA3, HSP101.