ArticleBiochimica et biophysica acta. Gene regulatory mechanisms2019
Oxoglutarate dehydrogenase and acetyl-CoA acyltransferase 2 selectively associate with H2A.Z-occupied promoters and are required for histone modifications.
Article in Biochimica et biophysica acta. Gene regulatory mechanisms, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Reducing branched-chain amino acids improves cardiac stress response in mice by decreasing histone H3K23 propionylation.The Journal of clinical investigation · 2023Article
- Negative correlation between acetyl-CoA acyltransferase 2 and cetuximab resistance in colorectal cancer.Acta biochimica et biophysica Sinica · 2023Article
- Review
- Dichloroacetate and thiamine improve survival and mitochondrial stress in a C. elegans model of dihydrolipoamide dehydrogenase deficiency.JCI insight · 2022Article
- The α-Ketoglutarate Dehydrogenase Complex as a Hub of Plasticity in Neurodegeneration and Regeneration.International journal of molecular sciences · 2022Review
- Targeting 2-oxoglutarate dehydrogenase for cancer treatment.American journal of cancer research · 2022Review
- ACAA2 is a ligand-dependent coactivator for thyroid hormone receptor β1.Biochemical and biophysical research communications · 2021Article
- The antiviral sirtuin 3 bridges protein acetylation to mitochondrial integrity and metabolism during human cytomegalovirus infection.PLoS pathogens · 2021Article
- Role of succinylation modification in thyroid cancer and breast cancer.American journal of cancer research · 2021Review
- Exclusive neuronal detection of KGDHC-specific subunits in the adult human brain cortex despite pancellular protein lysine succinylation.Brain structure & function · 2020Article
- Metabolism, Epigenetics, and Causal Inference in Heart Failure.Trends in endocrinology and metabolism: TEM · 2020Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Histone H2A.Z plays an essential role in regulating transcriptional rates and memory. Interestingly, H2A.Z-bound nucleosomes are located in both transcriptionally active and inactive promotors, with no clear understanding of the mechanisms via which it differentially regulates transcription. We hypothesized that its functions are mediated through recruitment of regulatory proteins to promoters. Using rapid chromatin immunoprecipitation-mass spectrometry, we uncovered the association of H2A.Z-bound chromatin with the metabolic enzymes, oxoglutarate dehydrogenase (OGDH) and acetyl-CoA acyltransferase 2 (ACAA2). Recombinant green florescence fusion proteins, combined with mutations of predicted nuclear localization signals, confirmed their nuclear localization and chromatin binding. Conclusively, chromatin immunoprecipitation-deep sequencing, confirmed the predominant association of OGDH and ACAA2 with H2A.Z-occupied transcription start sites and enhancers, the former of which we confirmed is conserved in both mouse and human tissue. Furthermore, H2A.Z-deficient human HAP1 cells exhibited reduced chromatin-bound metabolic enzymes, accompanied with reduced posttranslational histone modifications, including acetylation and succinylation. Specifically, knockdown of OGDH diminished H4 succinylation. Thus, the data reveal that select metabolic enzymes are assembled at active, H2A.Z-occupied, promoters, for potential site-directed production of metabolic intermediates that are required for histone modifications.
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