Ontology highlight
ABSTRACT:
SUBMITTER: Friis RM
PROVIDER: S-EPMC2709565 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
Friis R Magnus N RM Wu Bob P BP Reinke Stacey N SN Hockman Darren J DJ Sykes Brian D BD Schultz Michael C MC
Nucleic acids research 20090430 12
Little is known about what enzyme complexes or mechanisms control global lysine acetylation in the amino-terminal tails of the histones. Here, we show that glucose induces overall acetylation of H3 K9, 18, 27 and H4 K5, 8, 12 in quiescent yeast cells mainly by stimulating two KATs, Gcn5 and Esa1. Genetic and pharmacological perturbation of carbon metabolism, combined with (1)H-NMR metabolic profiling, revealed that glucose induction of KAT activity directly depends on increased glucose catabolis ...[more]