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SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications

ABSTRACT: SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications

PROVIDER: PRJNA1019665 | ENA |

REPOSITORIES: ENA

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SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications [RNA-seq]

Project description:Histone post-translational modifications (PTMs), such as acetylation and recently identified lysine 2-hydroxyisobutyrylation (Khib), act as active epigenomic marks in plants. SANT domain-containing proteins (SANT1/2/3/4), derived from PIF/Harbinger transposases, form a novel complex with histone deacetylase 6 (HDA6) to regulate gene expression via histone deacetylation. However, whether SANT1/2/3/4 coordinate different types of PTMs to regulate transcription and mediate responses to specific stresses in plants remain unclear. Here, in addition to modulating histone deacetylation, we found that SANT1/2/3/4 proteins acted like HDA6 or HDA9, in regulating the removal of histone Khib. H3KAc and histone Khib coordinated by SANT1/2/3/4 act in concert to regulate gene expression, with H3KAc playing a predominant role and Khib acting complementarily to H3KAc. SANT1/2/3/4 mutation significantly increased the expression of heat-inducible genes with concurrent change of H3KAc levels under normal and heat stress conditions, resulting in enhanced thermotolerance. Interestingly, hda6 mutant plants exhibited a reduced thermotolerance, suggesting that SANT1/2/3/4 negatively regulate plant thermotolerance independently of HDA6. This study revealed the critical roles of Harbinger transposon-derived SANT domain-containing proteins in transcriptional regulation by coordinating different types of histone PTMs and in the regulation of plant thermotolerance.

2025-09-01 | GSE243706 | GEO

SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications [ChIP-seq]

2025-09-01 | GSE243705 | GEO

SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications [RNA-seq]

Project description:SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications [RNA-seq]

| PRJNA1019667 | ENA

SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications [ChIP-seq]

Project description:SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications [ChIP-seq]

| PRJNA1019666 | ENA

SANT domain-containing proteins modulate gene transcription and negatively regulate plant thermotolerance by coordinating histone H3KAc and Khib modifications

Project description:This SuperSeries is composed of the SubSeries listed below.

2025-09-01 | GSE243707 | GEO

Thermotolerance in B. subtilis

2014-05-01 | GSE45972 | GEO

Assessment of Thermotolerance in preshocked hsp70(-/-) and (+/+) cells

Project description:From preliminary experiments, HSP70 deficient MEF cells display moderate thermotolerance to a severe heatshock of 45.5 degrees after a mild preshock at 43 degrees, even in the absence of hsp70 protein. We would like to determine which genes in these cells are being activated to account for this thermotolerance. Keywords: thermal stress, heat shock response, knockout, cell culture, hsp70

2009-04-09 | GSE11120 | GEO

Thermotolerance in B. subtilis

Project description:During thermotolerance development, B. subtilis cells can be primed by a short mild heat shock to survive a subsequent severe, otherwise lethal, heat stress. We wanted to assess the influence of transcriptional regulation during thermotolerance development in B. subtilis. We prepared total RNA of four differently treated samples of B. subtilis cells. For this purpose, exponential B. subtilis cells grown at 37 Â°C were divided and exposed for additional 15 min to temperatures of 37 Â°C, 48 Â°C, 53 Â°C or 15 min 48 Â°C followed by 15 min at 53 Â°C. Using four different merged dye swap experiments of red or green labelled cDNA of the above described RNA preparations, we compared and analyzed the transcriptional change of the conditions 48 Â°C vs. 53/48 Â°C (array 1), 37 Â°C vs. 53 Â°C (array 2), 37 Â°C vs. 48 Â°C (array 3) and especially 37/53Â°C vs. 53/48 Â°C (array 4)

2014-05-01 | E-GEOD-45972 | biostudies-arrayexpress

Unraveling the Mechanism of Thermotolerance in Cryptococcus neoformans by Set3C Complex

Project description:Thermotolerance, a key factor essential for the virulence of pathogenic fungi including Cryptococcus neoformans, remains largely unexplored in terms of its underlying mechanism. In this study, our findings demonstrate that Set3C, a widely distributed and conserved histone deacetylase complex, is required for thermotolerance in Cryptococcus neoformans. Specifically, the deletion of the core subunit Set302, responsible for the integrity of the complex, results in a significant reduction in the growth ability under high stress and the viability at extreme temperature. Moreover, the absence of Set302 leads to a decrease in the production of capsule and melanin. Transcriptomics analysis revealed that Set302 regulates a large number of genes compared to normal condition, and their expression is responsive to heat stress. Notably, we observed that Set302 positively influences the expression of genes related to ubiquitin-proteasome system (UPS) at high temperature. Using GFP-α-synuclein overexpression model, we observed a pronounced accumulation of misfolded proteins under heat stress, consequently inhibiting the thermotolerance of Cryptococcus neoformans. Furthermore, the loss of Set302 exacerbates this inhibition of thermotolerance. Interestingly, set302∆ strain exhibits a similar phenotype under proteasome stress as it does under high temperature. We also found that set302∆ strain displayed significantly reduced pathogenicity and colonization ability compared to the wild-type strain in the murine infection model. Collectively, our findings indicate that Set302 modulates the degradation of misfolded proteins through the UPS pathway, thereby affecting the thermotolerance and pathogenicity of Cryptococcus neoformans.

2023-09-05 | GSE242109 | GEO

Zebrafish embryos exposed to the model hedgehog pathway inhibitor cyclopamine, as well as to the potential hedghog pathway disrupters SANT-2 and GANT-61.

Project description:The hedgehog (Hh) signaling pathway is important for various developmental processes during embryogenesis and for homeostasis of adult tissue in vertebrates. Aberrant signaling results in severe birth defects and malignancies, respectively. The small molecules SANT-2 and GANT-61 were identified as potential Hh-pathway inhibitors in a reporter gene assay (Shh-light II cells). We aimed to analyze the effects of these compounds on the gene expression level in zebrafish embryos in comparison with the well known Hh-pathway inhibitor cyclopamine. Zebrafish embryos were treated with Ethanol (0,1%) (control), 10 µM Cyclopamine (C), 10 µM SANT-2 (S), and 10 µM GANT-61 (G), for 24 h (0.5 - 24 hpf), respectively; all in 5 independent replicates with 100 zebrafish embryos per treatment. Total RNA was extracted and processed as recommended by Agilent. One color arrays were used and data is given as normalized log2 of the gprocessed signals.

2011-09-30 | E-GEOD-29357 | biostudies-arrayexpress

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