Ontology highlight
ABSTRACT:
SUBMITTER: Wang ZA
PROVIDER: S-EPMC10071992 | biostudies-literature | 2023 Mar
REPOSITORIES: biostudies-literature
Wang Zhipeng A ZA Markert Jonathan W JW Whedon Samuel D SD Yapa Abeywardana Maheeshi M Lee Kwangwoon K Jiang Hanjie H Suarez Carolay C Lin Hening H Farnung Lucas L Cole Philip A PA
Journal of the American Chemical Society 20230317 12
The reversible acetylation of histone lysine residues is controlled by the action of acetyltransferases and deacetylases (HDACs), which regulate chromatin structure and gene expression. The sirtuins are a family of NAD-dependent HDAC enzymes, and one member, sirtuin 6 (Sirt6), influences DNA repair, transcription, and aging. Here, we demonstrate that Sirt6 is efficient at deacetylating several histone H3 acetylation sites, including its canonical site Lys9, in the context of nucleosomes but not ...[more]