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Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites

ABSTRACT: Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites

PROVIDER: PRJNA783022 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17021200.fastq.gz	Fastqsanger.gz
	SRR17021201.fastq.gz	Fastqsanger.gz
	SRR17021202.fastq.gz	Fastqsanger.gz
	SRR17021203.fastq.gz	Fastqsanger.gz
	SRR17021204.fastq.gz	Fastqsanger.gz

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Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (RNA-Seq)

Project description:Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (RNA-Seq)

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Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (ChIP-Seq)

Project description:Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (ChIP-Seq)

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Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (RNA-Seq)

Project description:Histone acetylation, a post-translational modification associated with transcriptional activation, is governed by nuclear acetyl-CoA pools that can vary depending on the metabolic state of the cell. The metabolic enzyme acetyl-CoA synthetase 2 (ACSS2) is proposed to regulate nuclear acetyl-CoA levels, using local acetate to produce acetyl-CoA that is utilized for histone acetylation. We hypothesize that during gene activation, a local transfer of intact acetate occurs between histones to upregulate transcription via sequential action of epigenetic and metabolic enzymes. Here we present converging lines of evidence in support of this acetate transfer to serve rapid gene induction. Using stable isotope labeling, we detect local transfer of intact acetate between histone acetylation sites both in vitro using purified mammalian enzymes and in vivo using quiescence exit in Saccharomyces cerevisiae as a change-of-state model. We delineate the enzymatic components required for this transfer mechanism, finding that ACSS2, histone deacetylase and histone acetyltransferase enzymes are necessary for efficient acetyl-group transfer in vitro. We show that Acs2, the yeast orthologue of ACSS2, is recruited to the genome during quiescence exit, and observe dynamic changes of histone acetylation in the vicinity of Acs2 peaks in vivo. Strikingly, we find that Acs2 is preferentially associated with the most upregulated growth genes, suggesting that acetyl-group transfer might play an important role in increased gene expression. Overall, our data reveal direct transfer of acetate between histone lysine residues to facilitate rapid transcriptional induction, an exchange that may be critical during metabolic alterations and changes in nutrient availability.

2022-01-21 | GSE189444 | GEO

Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (ChIP-Seq)

2022-01-21 | GSE189445 | GEO

Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites.

Project description:Histone acetylation is governed by nuclear acetyl-CoA pools generated, in part, from local acetate by metabolic enzyme acetyl-CoA synthetase 2 (ACSS2). We hypothesize that during gene activation, a local transfer of intact acetate occurs via sequential action of epigenetic and metabolic enzymes. Using stable isotope labeling, we detect transfer between histone acetylation sites both in vitro using purified mammalian enzymes and in vivo using quiescence exit in Saccharomyces cerevisiae as a change-of-state model. We show that Acs2, the yeast ortholog of ACSS2, is recruited to chromatin during quiescence exit and observe dynamic histone acetylation changes proximal to Acs2 peaks. We find that Acs2 is preferentially associated with the most up-regulated genes, suggesting that acetyl group transfer plays an important role in gene activation. Overall, our data reveal direct transfer of acetate between histone lysine residues to facilitate rapid transcriptional induction, an exchange that may be critical during changes in nutrient availability.

| S-EPMC8782443 | biostudies-literature

Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites

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

2022-01-21 | GSE189446 | GEO

LC-MS/MS identification of Kbz sites on histones catalyzed by non-enzymatic and enzymatic ways.

Project description:Histone lysine benzoylation may occur by Gcn5-catalyzed and nonenzymatically ways in vivo. In this project, we identified several Kbz sites on Xenopus laevis octamer in the absence or presence Gcn5-Ada2 complex in vitro, respectively. The number 672 represents the data in the absence of Gcn5-Ada2, and the number 674 represents the data that in the presence of Gcn5-Ada2.

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Project description:The lysine-specific demethylase 1 (LSD1) regulates hematopoietic stem cell differentiation and has been identified as a therapeutic target in hematological disorders. LSD1 demethylates mono and dimethylated histones 3 at lysine 4 and 9. In addition, it acts as a scaffold for the formation of chromatin-modifying complexes that regulates the transcription of myeloid-lineage-specific genes in complex with GFI1, a transcriptional repressor. While both enzymatic and non-enzymatic functions of LSD1 have been well defined, the relative importance of these two functions in hematopoiesis remains incompletely understood. Here, we investigated the contribution of enzymatic and non-enzymatic functions of LSD1 to myelopoiesis. We show that myeloid differentiation is independent of the enzymatic functions of LSD1 but requires the non-enzymatic, scaffolding function, which directs GFI1 binding to target sequences. In absence of the LSD1 protein, GFI1 DNA binding is diminished and myeloid cell differentiation arrests at a granulocyte-macrophage-progenitor-like cell stage, which overexpresses Prtn3. We provide functional data implicating Prtn3 as an effector of the stem cell expansion and myeloid maturation block caused by the loss of LSD1.

2025-08-12 | GSE286396 | GEO

Lysine-specific demethylase 1 regulates hematopoietic stem cell expansion and myeloid cell differentiation [scRNA-seq]

Project description:The lysine-specific demethylase 1 (LSD1) regulates hematopoietic stem cell differentiation and has been identified as a therapeutic target in hematological disorders. LSD1 demethylates mono and dimethylated histones 3 at lysine 4 and 9. In addition, it acts as a scaffold for the formation of chromatin-modifying complexes that regulates the transcription of myeloid-lineage-specific genes in complex with GFI1, a transcriptional repressor. While both enzymatic and non-enzymatic functions of LSD1 have been well defined, the relative importance of these two functions in hematopoiesis remains incompletely understood. Here, we investigated the contribution of enzymatic and non-enzymatic functions of LSD1 to myelopoiesis. We show that myeloid differentiation is independent of the enzymatic functions of LSD1 but requires the non-enzymatic, scaffolding function, which directs GFI1 binding to target sequences. In absence of the LSD1 protein, GFI1 DNA binding is diminished and myeloid cell differentiation arrests at an immature, myelomonocytic-like cell stage, which overexpresses Prtn3. We provide functional data implicating Prtn3 as an effector of the stem cell expansion and myeloid maturation block caused by the loss of LSD1.

2025-08-12 | GSE286398 | GEO

Expression data from wild-type and H2B K37A mutant yeast histones

Project description:We identified lysine 37 of histone H2B as a novel site of histone lysine methylation in budding yeast. Microarray analysis was performed to determine global changes in gene expression upon mutation of this lysine residue to a unmodifiable form. Histones were acid-extracted from asynchronously grown yeast expressing wild-type H2B or H2B harboring a K37A mutation.

2010-09-26 | E-GEOD-24380 | biostudies-arrayexpress

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