Ontology highlight
ABSTRACT:
SUBMITTER: Zheng Y
PROVIDER: S-EPMC3929392 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Zheng Yupeng Y Thomas Paul M PM Kelleher Neil L NL
Nature communications 20130101
Histone acetylation has long been determined as a highly dynamic modification associated with open chromatin and transcriptional activation. Here we develop a metabolic labelling scheme using stable isotopes to study the kinetics of acetylation turnover at 19 distinct lysines on histones H3, H4 and H2A. Using human HeLa S3 cells, the analysis reveals 12 sites of histone acetylation with fast turnover and 7 sites stable over a 30 h experiment. The sites showing fast turnover (anticipated from cla ...[more]