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Nuclear Pyruvate Dehydrogenase Complex regulates EIN2-directed Histone Acetylation and Transcriptional Regulation in the Ethylene Response.

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE212540 | GEO | 2023/12/01

REPOSITORIES: GEO

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Nuclear Pyruvate Dehydrogenase Complex regulates EIN2-directed Histone Acetylation and Transcriptional Regulation in the Ethylene Response.[ChIP-Seq]

Project description:Next-generation sequencing (NGS) has been used to study the histone acetylation in Arabidopsis etiolated seedlings under air and ethylene treatment. The goal of this study is to investigate how pyruvate dehydrogenase complex is involved in histone acetylation changes in response to ethylene.

2023-12-01 | GSE212536 | GEO

Nuclear Pyruvate Dehydrogenase Complex regulates EIN2-directed Histone Acetylation and Transcriptional Regulation in the Ethylene Response. [RNA-Seq]

Project description:Next-generation sequencing (NGS) has been used to study the differential gene expression in Arabidopsis etiolated seedlings under air and ethylene treatment. The goal of this study is to investigate how pyruvate dehydrogenase complex is involved in transcriptional regulation in response to ethylene.

2023-12-01 | GSE212530 | GEO

Nuclear Pyruvate Dehydrogenase Complex regulates EIN2-directed Histone Acetylation and Transcriptional Regulation in the Ethylene Response.

Project description:Histone acetylation is important for the transcriptional regulation in the ethylene response and the nuclear metabolic production of acetyl coenzyme A (acetyl-CoA) plays key roles in histone acetylation. But how the nucleus produces acetyl-CoA for histone acetylation and transcription regulation in the ethylene response is completely unknown. Here we show that functional pyruvate dehydrogenase complex (PDC) translocates from the mitochondria to the nucleus in response to ethylene, generating nuclear acetyl CoA from pyruvate to regulate EIN2-directed histone acetylation and transcription in the target genes. It has been reported that the dephosphorylated E1 subunit of the PDC complex is required for the PDC activity, we examined the phosphorylation status change of E1 in the nucleus in response to ethylene. The MS data shows quantitative phosphorylation differences between cytosolic and nuclear fraction supporting the dephosphorylation of E1 upon ethylene treatment.

2024-06-25 | PXD040689 | Pride

EIN2 mediates direct regulation of histone acetylation in the ethylene response.

Project description:Ethylene gas is essential for developmental processes and stress responses in plants. Although the membrane-bound protein EIN2 is critical for ethylene signaling, the mechanism by which the ethylene signal is transduced remains largely unknown. Here we show the levels of H3K14Ac and H3K23Ac are correlated with the levels of EIN2 protein and demonstrate EIN2 C terminus (EIN2-C) is sufficient to rescue the levels of H3K14/23Ac of ein2-5 at the target loci, using CRISPR/dCas9-EIN2-C. Chromatin immunoprecipitation followed by deep sequencing (ChIP-seq) and ChIP-reChIP-seq analyses revealed that EIN2-C associates with histone partially through an interaction with EIN2 nuclear-associated protein1 (ENAP1), which preferentially binds to the genome regions that are associated with actively expressed genes both with and without ethylene treatments. Specifically, in the presence of ethylene, ENAP1-binding regions are more accessible upon the interaction with EIN2, and more EIN3 proteins bind to the loci where ENAP1 is enriched for a quick response. Together, these results reveal EIN2-C is the key factor regulating H3K14Ac and H3K23Ac in response to ethylene and uncover a unique mechanism by which ENAP1 interacts with chromatin, potentially preserving the open chromatin regions in the absence of ethylene; in the presence of ethylene, EIN2 interacts with ENAP1, elevating the levels of H3K14Ac and H3K23Ac, promoting more EIN3 binding to the targets shared with ENAP1 and resulting in a rapid transcriptional regulation.

| S-EPMC5617289 | biostudies-literature

EIN2-dependent regulation of acetylation of histone H3K14 and non-canonical histone H3K23 in ethylene signalling.

Project description:Ethylene gas is essential for many developmental processes and stress responses in plants. EIN2 plays a key role in ethylene signalling but its function remains enigmatic. Here, we show that ethylene specifically elevates acetylation of histone H3K14 and the non-canonical acetylation of H3K23 in etiolated seedlings. The up-regulation of these two histone marks positively correlates with ethylene-regulated transcription activation, and the elevation requires EIN2. Both EIN2 and EIN3 interact with a SANT domain protein named EIN2 nuclear associated protein 1 (ENAP1), overexpression of which results in elevation of histone acetylation and enhanced ethylene-inducible gene expression in an EIN2-dependent manner. On the basis of these findings we propose a model where, in the presence of ethylene, the EIN2 C terminus contributes to downstream signalling via the elevation of acetylation at H3K14 and H3K23. ENAP1 may potentially mediate ethylene-induced histone acetylation via its interactions with EIN2 C terminus.

| S-EPMC5063967 | biostudies-literature

Mitochondrial carrier homolog 2 (MTCH2) regulates the differentiation of AML cells by controlling pyruvate entry into the mitochondria, nuclear localization of pyruvate dehydrogenase complex and H3 and H4 histone acetylation

Project description:Inhibiting MTCH2 or the Mitochondrial Pyruvate Carrier increased levels of pyruvate and pyruvate dehydrogenase in the nucleus leading to differentiation and loss of stemness in AML.

2020-09-01 | GSE103834 | GEO

Methylation-directed acetylation of histone H3 regulates developmental sensitivity to histone deacetylase inhibition.

Project description:Hydroxamate-based lysine deacetylase inhibitors (KDACis) are approved for clinical use against certain cancers. However, intrinsic and acquired resistance presents a major problem. Treatment of cells with hydroxamates such as trichostatin A (TSA) leads to rapid preferential acetylation of histone H3 already trimethylated on lysine 4 (H3K4me3), although the importance of this H3K4me3-directed acetylation in the biological consequences of KDACi treatment is not known. We address this utilizing Dictyostelium discoideum strains lacking H3K4me3 due to disruption of the gene encoding the Set1 methyltransferase or mutations in endogenous H3 genes. Loss of H3K4me3 confers resistance to TSA-induced developmental inhibition and delays accumulation of H3K9Ac and H3K14Ac. H3K4me3-directed H3Ac is mediated by Sgf29, a subunit of the SAGA acetyltransferase complex that interacts with H3K4me3 via a tandem tudor domain (TTD). We identify an Sgf29 orthologue in Dictyostelium with a TTD that specifically recognizes the H3K4me3 modification. Disruption of the gene encoding Sgf29 delays accumulation of H3K9Ac and abrogates H3K4me3-directed H3Ac. Either loss or overexpression of Sgf29 confers developmental resistance to TSA. Our results demonstrate that rapid acetylation of H3K4me3 histones regulates developmental sensitivity to TSA. Levels of H3K4me3 or Sgf29 will provide useful biomarkers for sensitivity to this class of chemotherapeutic drug.

| S-EPMC8053100 | biostudies-literature

EIN2 mediates histone H3K14 and non-canonical histone H3K23 acetylation in the nucleus in ethylene response

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

2016-10-04 | GSE77396 | GEO

Acetylation of histone deacetylase 1 regulates NuRD corepressor complex activity.

Project description:BackgroundHDAC1-containing NuRD complex is required for GATA-1-mediated repression and activation.ResultsGATA-1 associated with acetylated HDAC1-containing NuRD complex, which has no deacetylase activity, for gene activation.ConclusionAcetylated HDAC1 converts NuRD complex from a repressor to an activator during GATA-1-directed erythroid differentiation program.SignificanceHDAC1 acetylation may function as a master regulator for the activity of HDAC1 containing complexes. Histone deacetylases (HDACs) play important roles in regulating cell proliferation and differentiation. The HDAC1-containing NuRD complex is generally considered as a corepressor complex and is required for GATA-1-mediated repression. However, recent studies also show that the NuRD complex is involved in GATA-1-mediated gene activation. We tested whether the GATA-1-associated NuRD complex loses its deacetylase activity and commits the GATA-1 complex to become an activator during erythropoiesis. We found that GATA-1-associated deacetylase activity gradually decreased upon induction of erythroid differentiation. GATA-1-associated HDAC1 is increasingly acetylated after differentiation. It has been demonstrated earlier that acetylated HDAC1 has no deacetylase activity. Indeed, overexpression of an HDAC1 mutant, which mimics acetylated HDAC1, promotes GATA-1-mediated transcription and erythroid differentiation. Furthermore, during erythroid differentiation, acetylated HDAC1 recruitment is increased at GATA-1-activated genes, whereas it is significantly decreased at GATA-1-repressed genes. Interestingly, deacetylase activity is not required for Mi2 remodeling activity, suggesting that remodeling activity may be required for both activation and repression. Thus, our data suggest that NuRD can function as a coactivator or repressor and that acetylated HDAC1 converts the NuRD complex from a repressor to an activator during GATA-1-directed erythroid differentiation.

| S-EPMC3504744 | biostudies-literature

EIN2 mediates histone H3K14 and non-canonical histone H3K23 acetylation in the nucleus in ethylene response [RNA-seq]

Project description:We report that ENAP1 interacts with EIN3CEND and histone H3, and enhances histone acetylation. We examined the gene expression in ENAP1ox lines, compared with that in COL lines.

2016-10-05 | GSE77395 | GEO

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