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

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

Authors

  • Takahashi H
  • McCaffery JM
  • Irizarry RA
  • Boeke JD

Journal

Molecular cell

Publication Data

July 21, 2006

Associated Grants

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

Mesh Terms

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