Papers

Peer-reviewed
Feb, 2016

SMARCAD1 is an ATP-dependent stimulator of nucleosomal H2A acetylation via CBP, resulting in transcriptional regulation

SCIENTIFIC REPORTS
  • Masamichi Doiguchi
  • Takeya Nakagawa
  • Yuko Imamura
  • Mitsuhiro Yoneda
  • Miki Higashi
  • Kazuishi Kubota
  • Satoshi Yamashita
  • Hiroshi Asahara
  • Midori Iida
  • Satoshi Fujii
  • Tsuyoshi Ikura
  • Ziying Liu
  • Tulip Nandu
  • W. Lee Kraus
  • Hitoshi Ueda
  • Takashi Ito
  • Display all

Volume
6
Number
First page
20179
Last page
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1038/srep20179
Publisher
NATURE PUBLISHING GROUP

Histone acetylation plays a pivotal role in transcriptional regulation, and ATP-dependent nucleosome remodeling activity is required for optimal transcription from chromatin. While these two activities have been well characterized, how they are coordinated remains to be determined. We discovered ATP-dependent histone H2A acetylation activity in Drosophila nuclear extracts. This activity was column purified and demonstrated to be composed of the enzymatic activities of CREB-binding protein (CBP) and SMARCAD1, which belongs to the Etl1 subfamily of the Snf2 family of helicase-related proteins. SMARCAD1 enhanced acetylation by CBP of H2A K5 and K8 in nucleosomes in an ATP-dependent fashion. Expression array analysis of S2 cells having ectopically expressed SMARCAD1 revealed up-regulated genes. Using native genome templates of these up-regulated genes, we found that SMARCAD1 activates their transcription in vitro. Knockdown analysis of SMARCAD1 and CBP indicated overlapping gene control, and ChIP-seq analysis of these commonly controlled genes showed that CBP is recruited to the promoter prior to SMARCAD1. Moreover, Drosophila genetic experiments demonstrated interaction between SMARCAD1/Etl1 and CBP/nej during development. The interplay between the remodeling activity of SMARCAD1 and histone acetylation by CBP sheds light on the function of chromatin and the genome-integrity network.

Link information
DOI
https://doi.org/10.1038/srep20179
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/26888216
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000370341400001&DestApp=WOS_CPL
ID information
  • DOI : 10.1038/srep20179
  • ISSN : 2045-2322
  • Pubmed ID : 26888216
  • Web of Science ID : WOS:000370341400001

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