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• W2045720893 abstract "Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment. However, because nucleocytosolic acetyl-CoA is also used for de novo synthesis of fatty acids, histone acetylation and synthesis of fatty acids compete for the same acetyl-CoA pool. The first and rate-limiting reaction in de novo synthesis of fatty acids is carboxylation of acetyl-CoA to form malonyl-CoA, catalyzed by acetyl-CoA carboxylase. In yeast Saccharomyces cerevisiae, acetyl-CoA carboxylase is encoded by the ACC1 gene. In this study, we show that attenuated expression of ACC1 results in increased acetylation of bulk histones, globally increased acetylation of chromatin histones, and altered transcriptional regulation. Together, our data indicate that Acc1p activity regulates the availability of acetyl-CoA for histone acetyltransferases, thus representing a link between intermediary metabolism and epigenetic mechanisms of transcriptional regulation.Background: Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment.Results: Attenuated expression of acetyl-CoA carboxylase, the first and rate-limiting enzyme in de novo fatty acid synthesis, results in increased histone acetylation.Conclusion: Fatty acid biosynthesis competes with histone acetylation for acetyl-CoA.Significance: Intermediary metabolism affects histone acetylation and transcriptional regulation. Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment. However, because nucleocytosolic acetyl-CoA is also used for de novo synthesis of fatty acids, histone acetylation and synthesis of fatty acids compete for the same acetyl-CoA pool. The first and rate-limiting reaction in de novo synthesis of fatty acids is carboxylation of acetyl-CoA to form malonyl-CoA, catalyzed by acetyl-CoA carboxylase. In yeast Saccharomyces cerevisiae, acetyl-CoA carboxylase is encoded by the ACC1 gene. In this study, we show that attenuated expression of ACC1 results in increased acetylation of bulk histones, globally increased acetylation of chromatin histones, and altered transcriptional regulation. Together, our data indicate that Acc1p activity regulates the availability of acetyl-CoA for histone acetyltransferases, thus representing a link between intermediary metabolism and epigenetic mechanisms of transcriptional regulation. Background: Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment. Results: Attenuated expression of acetyl-CoA carboxylase, the first and rate-limiting enzyme in de novo fatty acid synthesis, results in increased histone acetylation. Conclusion: Fatty acid biosynthesis competes with histone acetylation for acetyl-CoA. Significance: Intermediary metabolism affects histone acetylation and transcriptional regulation." @default.
• W2045720893 created "2016-06-24" @default.
• W2045720893 creator A5019782659 @default.
• W2045720893 creator A5071871609 @default.
• W2045720893 date "2012-07-01" @default.
• W2045720893 modified "2023-10-03" @default.
• W2045720893 title "Acetyl-CoA Carboxylase Regulates Global Histone Acetylation" @default.
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• W2045720893 doi "https://doi.org/10.1074/jbc.m112.380519" @default.
• W2045720893 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3390662" @default.
• W2045720893 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22580297" @default.
• W2045720893 hasPublicationYear "2012" @default.
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