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Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription.

Molecular cell | Jul 21, 2006

http://www.ncbi.nlm.nih.gov/pubmed/16857587

Metabolic enzymes rarely regulate informational processes like gene expression. Yeast acetyl-CoA synthetases (Acs1p and 2p) are exceptional, as they are important not only for carbon metabolism but also are shown here to supply the acetyl-CoA for histone acetylation by histone acetyltransferases (HATs). acs2-Ts mutants exhibit global histone deacetylation, transcriptional defects, and synthetic growth defects with HAT mutants at high temperatures. In glycerol with ethanol, Acs1p is an alternate acetyl-CoA source for HATs. Rapid deacetylation after Acs2p inactivation suggests nuclear acetyl-CoA synthesis is rate limiting for histone acetylation. Different histone lysines exhibit distinct deacetylation rates, with N-terminal tail lysines deacetylated rapidly and H3 lysine 56 slowly. Yeast mitochondrial and nucleocytosolic acetyl-CoA pools are biochemically isolated. Thus, acetyl-CoA metabolism is directly linked to chromatin regulation and may affect diverse cellular processes in which acetylation and metabolism intersect, such as disease states and aging.

Pubmed ID: 16857587 RIS Download

Mesh terms: Acetate-CoA Ligase | Acetylation | Cell Nucleus | Coenzyme A Ligases | Cytosol | Histone Acetyltransferases | Histones | Mitochondria | Mutation | Saccharomyces cerevisiae Proteins | Signal Transduction | Transcription, Genetic

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM62385
  • Agency: NCRR NIH HHS, Id: RR020839
  • Agency: NCRR NIH HHS, Id: S10 RR019409-01

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