Metabolic control of methylation and acetylation.

TitleMetabolic control of methylation and acetylation.
Publication TypeJournal Article
Year of Publication2016
AuthorsSu, X, Wellen, KE, Rabinowitz, JD
JournalCurr Opin Chem Biol
Volume30
Pagination52-60
Date Published2016 Feb
ISSN1879-0402
KeywordsAcetylation, Animals, DNA, Epigenesis, Genetic, Histones, Humans, Methylation, Microbiology
Abstract

<p>Methylation and acetylation of DNA and histone proteins are the chemical basis for epigenetics. From bacteria to humans, methylation and acetylation are sensitive to cellular metabolic status. Modification rates depend on the availability of one-carbon and two-carbon substrates (S-adenosylmethionine, acetyl-CoA, and in bacteria also acetyl-phosphate). In addition, they are sensitive to demodification enzyme cofactors (α-ketoglutarate, NAD(+)) and structural analog metabolites that function as epigenetic enzyme inhibitors (e.g., S-adenosylhomocysteine, 2-hydroxyglutarate). Methylation and acetylation likely initially evolved to tailor protein activities in microbes to their metabolic milieu. While the extracellular environment of mammals is more tightly controlled, the combined impact of nutrient abundance and metabolic enzyme expression impacts epigenetics in mammals sufficiently to drive important biological outcomes such as stem cell fate and cancer. </p>

DOI10.1016/j.cbpa.2015.10.030
Alternate JournalCurr Opin Chem Biol
PubMed ID26629854
PubMed Central IDPMC4731252
Grant ListCA194973 / CA / NCI NIH HHS / United States
CA174761 / CA / NCI NIH HHS / United States
AI097382 / AI / NIAID NIH HHS / United States
R01 CA163591 / CA / NCI NIH HHS / United States
CA163591 / CA / NCI NIH HHS / United States
P30DK019525 / DK / NIDDK NIH HHS / United States
R01 AI097382 / AI / NIAID NIH HHS / United States
P30 DK019525 / DK / NIDDK NIH HHS / United States