Abstract
Histone deacetylase activity plays an important role in transcriptional repression. Botrytis cinerea is an important necrotrophic fungal pathogen distributed worldwide and parasites a wide range of hosts. However, the molecular mechanisms of how B. cinerea regulates growth and host infection remain largely unknown. Here, the function of BcRPD3, a histone deacetylase of B. cinerea, was investigated. Overexpression of the BcRPD3 gene resulted in significantly decreased acetylation levels of histone H3 and H4. The BcRPD3 overexpression strains showed slightly delayed vegetative growth, dramatically impaired infection structure formation, oxidative stress response, and virulence. RNA-Seq analysis revealed that enzymatic activity related genes, including 9 genes reported to function as virulence factors, were downregulated in BcRPD3 overexpression strain. Chromatin immunoprecipitation followed by qPCR confirmed the enrichment of BcRPD3 and H3Kac at the promoter regions of these nine genes. These observations indicated that BcRPD3 regulated the transcription of enzymatic activity related genes by controlling the acetylation level of histones, thereby affecting the vegetative growth, infection structure formation, oxidative stress response, and virulence of B. cinerea.
Highlights
Chromatin remodeling through histone acetylation is an important epigenetic mechanism controlling gene transcription
Fungal orthologs of RPD3 are found among necrotrophic fungi (Botrytis cinerea, Colletotrichum incanum, Aspergillus fumigatus), biotrophic fungi (Blumeria graminis, Melampsora larici-populina, Sporisorium reilianum, Bipolaris zeicola, Magnaporthe oryzae, Fusarium graminearum, Ustilago maydis), and yeasts (Cyberlindnera jadinii, Kluyveromyces marxianus, Zygosaccharomyces bailii, Saccharomyces cerevisiae)
This transcription pattern implicated that BcRPD3 was more active during vegetative growth phase than during plant infectious stages in B. cinerea, indicating that BcRPD3
Summary
Chromatin remodeling through histone acetylation is an important epigenetic mechanism controlling gene transcription. Histone hyperacetylation results in a loose chromatin structure and transcription activation, while hypoacetylation of histones leads to transcriptional repression by chromatin condensation. The acetylation of histones is antagonistically controlled by histone acetyltransferases (HATs) and histone deacetylases (HDACs) (Lee and Workman, 2007). Characterizing functions of HATs and HDACs is an important way to clarify the roles of histone acetylation. HDACs are a family of enzymes that reverse lysine acetylation catalyzed by HATs through deacetylation of lysine residues on histones. Except for its important roles in the epigenetic regulation of gene expression, recent studies have uncovered a plethora of non-histone targets
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