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Histone acetyl transferase (HAT) and APSES TF of Aspergillus fumigatus

ABSTRACT: Histone acetyl transferase (HAT) and APSES TF of Aspergillus fumigatus

PROVIDER: PRJNA757944 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15616557.fastq.gz	Fastqsanger.gz
	SRR15616558.fastq.gz	Fastqsanger.gz
	SRR15616559.fastq.gz	Fastqsanger.gz
	SRR15616560.fastq.gz	Fastqsanger.gz
	SRR15616561.fastq.gz	Fastqsanger.gz

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Histone acetyl transferase (HAT) and APSES TF of Aspergillus fumigatus

Project description:Transcriptome analysis of deletion mutant which coding HAT and APSES TF compared to wild type by NGS

2021-08-28 | GSE182799 | GEO

MOF acetyl transferase regulates transcription and respiration in mitochondria

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MOF acetyl transferase regulates transcription and respiration in mitochondria

Project description:Histone acetylation is sensitive to metabolic cues, however interplay between histone acetyl transferases and cellular metabolism remains poorly understood. Here we report the localization of a classical nuclear HAT- MOF and members of Non-Specific Lethal complex in mitochondria. MOF regulates expression of oxidative phosphorylation (OXPHOS) genes, residing in both nuclear and mitochondrial genomes, selectively in aerobically respiring cells. Furthermore, MOF/KANSL1 depletion causes impaired mitochondrial translation and reduced respiration. MOF loss is catastrophic for tissues with high-energy consumption. In mouse hearts, Mof knockout causes hypertrophic cardiomyopathy, compromised ventricular contractility/ stroke volume and ultimately leads to cardiac failure within three weeks of birth. RNA-seq analysis of the cardiomyocytes revealed deregulation of mitochondrial nutrient metabolism and OXPHOS pathways. Consistently, electron microscopy on affected tissues revealed mitochondrial deterioration with high tissue heterogeneity, commonly observed in mitochondrial diseases. Thus, we reveal a novel function of MOF in mitochondrial homeostasis and propose MOF as a sensor connecting epigenetic regulation to metabolism. We generated mRNA-seq profile of Mof depleted HeLa cells adapted in glucose or galactose media. We also present nuclear RNA seq profile from Mof deleted cardiomyocytes.

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Distinct contributions of KAT2A histone acetyl-transferase complexes to human erythropoiesis

Project description:Distinct contributions of KAT2A histone acetyl-transferase complexes to human erythropoiesis

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A Curcumin-Based CBP HAT Inhibitor Modulates the Transcription Functions of Tumor Suppressor p53

Project description:Coactivator CREB-binding protein (CBP) regulates the transcription program of p53, which orchestrates cellular responses to a wide-range of stress conditions that cause genomic instability. Given the ability of CBP to regulate transcription by multiple mechanisms, the biological significance of its acetylation-directed functions may not be fully clear. The present study demonstrates the development of a curcumin-derived modulator of CBP histone acetyl-transferase (HAT) activity, CM354, which inhibits acetylation of p53 on lysine 382, acetylation of histone H3K27 and autoacetylation of CBP. These epigenetic changes are concomitant with downregulation of p53 and CBP functions, which facilitate the presence of histone methyl transferase, Enhancer of zeste homolog 2 (EZH2), on CDKNI1A/p21 promoter, thereby, enhancing the level of trimethylation on H3K27. Treatment with CM354 results in the activation of PARP and the abrogation of cellular growth. Genome-wide network analysis depicts that CM354 could alter cell-fate by enrichment of chromatin H3K27 methylation and activation of the polycomb group of proteins. Though previously reported HAT inhibitors act at higher concentrations and lack cell permeability, the present study shows the impact of modulating endogenous CBP HAT activity on chromatin landscape and p53 functions.

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MOF acetyl transferase regulates transcription and respiration in mitochondria

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Sequencing of proximal tubular carnitine-acetyl transferase knockout kidney cortex from mouse

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Distinct contributions of KAT2A histone acetyl-transferase complexes to human erythropoiesis [RNA-seq]

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Sequencing of proximal tubular carnitine-acetyl transferase Heterozygous knockout kidney cortex from mouse

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Distinct contributions of KAT2A histone acetyl-transferase complexes to human erythropoiesis

Project description:KAT2A is a histone acetyl-transferase involved in stabilization of transcriptional activity through acetylation of lysine residue 9 of Histone 3. Mouse knockout models suggest that Kat2a is dispensable for haematopoietic stem and progenitor cell activity, despite a central role in survival and maintenance of Acute Myekoid Leukaemia cells through block of differentiation. Herein, we investigate KAT2A activity in human cord blood haematopoiesis and identify a specific requirement in the establishment of the erythroid lineage. KAT2A is required for specification and survival of Erythroid-Megakaryocytic progenitors, with regulation of expression of the erythropoietin receptor (EPOR) gene, which participates in lineage commitment, as well as of later effector genes in the platelet and erythroid lineages. Early and late lineage roles can be distinctly attributed to the ATAC and SAGA complexes in which context KAT2A exerts its activity. ATAC is active earlier in erythroid lineage development and mediates MEP specification from HSC, whilst SAGA activity is required post-commitment, including in expression of haemoglobin genes. We thus position KAT2A as a novel regulator of human erythropoiesis and separate early and later effects in lineage development with complex specificity. This has implications for putative therapeutic targeting of KAT2A complexes in leukaemia.

2021-09-28 | GSE128512 | GEO

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