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Enhancer of Acetyltransferase Chameau (EAChm) Is a Novel Transcriptional Co-Activator
Authors:Takeya Nakagawa  Tsuyoshi Ikehara  Masamichi Doiguchi  Yuko Imamura  Miki Higashi  Mitsuhiro Yoneda  Takashi Ito
Affiliation:Department of Biochemistry, Nagasaki University School of Medicine, Nagasaki, 852–8523, Japan.; St. Georges University of London, UNITED KINGDOM,
Abstract: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. EAChm is a negatively charged acidic protein retaining aspartate and glutamate. Furthermore, we identified that Chameau and EAChm stimulate transcription in vitro together with purified general transcription factors. In addition, RNA-seq analysis of Chameu KD and EAChm KD S2 cells suggest that Chameau and EAChm regulate transcription of common genes in vivo. Our results suggest that EAChm regulates gene transcription in Drosophila embryos by enhancing Acetyltransferase Chameau activity.
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