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Essential angiosperm-specific subunits of HDA19 histone deacetylase complexes in Arabidopsis [ChIP-Seq]

ABSTRACT: Although the Arabidopsis thaliana histone deacetylase HDA19 and its close homolog HDA6 form SIN3-type histone deacetylase complexes, they display distinct biological roles, with the reason for these differences being poorly understood. We has identified three angiosperm-specific HDA19-interacting homologous proteins, termed HDIP1, HDIP2, and HDIP3 (HDIP1/2/3). These proteins interact with HDA19 and other conserved histone deacetylase complex components, leading to the formation of HDA19-containing SIN3-type complexes, while they are not involved in the formation of HDA6-containing ones. While mutants of conserved SIN3-type complex components show phenotypes divergent from the hda19 mutant, the hdip1/2/3 mutant closely mirrors the hda19 mutant in development, abscisic acid signaling, and drought stress tolerance. Omics analyses indicate that HDIP1/2/3 and HDA19 co-occupy chromatin and jointly repress gene transcription, especially for stress-related genes. An α-helix motif within HDIP1 has the capacity to bind to nucleosomes and architectural DNA, and is required for its function in Arabidopsis plants. These findings suggest that the angiosperm SIN3-type complexes have evolved to include additional subunits for the precise regulation of histone deacetylation and gene transcription.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE275986 | GEO | 2025/02/28

REPOSITORIES: GEO

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Angiosperm-specific subunits of histone deacetylase complexes are required for the functional specificities of the histone deacetylase HDA19 in development and stress responses [RNA-seq]

Project description:While both the histone deacetylase HDA19 and its close homolog HDA6 can form SIN3-type histone deacetylase complexes, they display specialized biological roles, with the mechanisms of their functional specificities largely unclear. In this study, we identified three previously uncharacterized homologs designated as HDA19-interacting proteins 1, 2, and 3 (HDIP1/2/3). These homologs not only interact with HDA19 but also with other components of the SIN3-type histone deacetylase complexes, including SNLs, MSI1, and HDC1, thereby facilitating the assembly of HDA19-containing complexes but not HDA6-containing ones. HDIP1/2/3 orthologs are found in angiosperms but are absent in other plant species. The hdip1/2/3 and hda19 mutants exhibit highly similar phenotypes in terms of development, abscisic acid response, and drought tolerance. Omics data indicate that HDIP1/2/3 and HDA19 co-occupy chromatin and co-repress gene transcription, particularly at those genes associated with stress responses. An a-helix motif in HDIP1 is capable of binding to the nucleosome as well as the four-way junction DNA that mimics the DNA entry and exit sites of the nucleosome, and is essential for the function of HDIP1 in Arabidopsis plants. These findings suggest that the HDA19-containing SIN3-type histone deacetylase complexes have incorporated additional subunits in angiosperms to support the intricate regulation of histone deacetylation and gene transcription during plant development and stress responses.

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