Ontology highlight
ABSTRACT:
SUBMITTER: Nakagawa T
PROVIDER: S-EPMC4640846 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Nakagawa Takeya T Ikehara Tsuyoshi T Doiguchi Masamichi M Imamura Yuko Y Higashi Miki M Yoneda Mitsuhiro M Ito Takashi T
PloS one 20151110 11
Acetylation of nucleosomal histones by diverse histone acetyltransferases (HAT) plays pivotal roles in many cellular events. Discoveries of novel HATs and HAT related factors have provided new insights to understand the roles and mechanisms of histone acetylation. In this study, we identified prominent Histone H3 acetylation activity in vitro and purified its activity, showing that it is composed of the MYST acetyltransferase Chameau and Enhancer of the Acetyltransferase Chameau (EAChm) family. ...[more]