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ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation

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Listed:
  • Hiroaki Kawasaki

    (Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN)
    National Institute for Advanced Interdisciplinary Research and National Institute of Bioscience and Human Technology, Agency of Industrial Science & Technology, MITI)

  • Lou Schiltz

    (Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health)

  • Robert Chiu

    (School of Medicine/School of Dentistry, Surgical Oncology/Oral Biology and Medicine, University of California)

  • Keiichi Itakura

    (Beckman Research Institute of the City of Hope)

  • Kazunari Taira

    (National Institute for Advanced Interdisciplinary Research and National Institute of Bioscience and Human Technology, Agency of Industrial Science & Technology, MITI
    Graduate School of Engineering, University of Tokyo)

  • Yoshihiro Nakatani

    (Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health
    Dana-Farber Cancer Institute)

  • Kazunari K. Yokoyama

    (Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN))

Abstract

Transcription factors carry functional domains, which are often physically distinct, for sequence-specific DNA binding, transcriptional activation and regulatory functions. The transcription factor ATF-2 is a DNA-binding protein that binds to cyclic AMP-response elements (CREs), forms a homodimer or heterodimer with c-Jun, and stimulates CRE-dependent transcription1,2,3. Here we report that ATF-2 is a histone acetyltransferase (HAT), which specifically acetylates histones H2B and H4 in vitro. Motif A, which is located in the HAT domain, is responsible for the stimulation of CRE-dependent transcription; moreover, in response to ultraviolet irradiation, phosphorylation of ATF-2 is accompanied by enhanced HAT activity of ATF-2 and CRE-dependent transcription. These results indicate that phosphorylation of ATF-2 controls its intrinsic HAT activity and its action on CRE-dependent transcription. ATF-2 may represent a new class of sequence-specific factors, which are able to activate transcription by direct effects on chromatin components.

Suggested Citation

  • Hiroaki Kawasaki & Lou Schiltz & Robert Chiu & Keiichi Itakura & Kazunari Taira & Yoshihiro Nakatani & Kazunari K. Yokoyama, 2000. "ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation," Nature, Nature, vol. 405(6783), pages 195-200, May.
    • Handle: RePEc:nat:nature:v:405:y:2000:i:6783:d:10.1038_35012097
    DOI: 10.1038/35012097
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