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Letters to Nature

Nature 405, 195-200 (11 May 2000) | doi:10.1038/35012097; Received 8 December 1999; Accepted 22 February 2000

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

Hiroaki Kawasaki1,2, Lou Schiltz3, Robert Chiu4, Keiichi Itakura, Kazunari Taira6,2, Yoshihiro Nakatani3,7 & Kazunari K. Yokoyama1

  1. Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), Tsukuba 305-0074, Japan
  2. National Institute for Advanced Interdisciplinary Research and National Institute of Bioscience and Human Technology, Agency of Industrial Science & Technology, MITI, Tsukuba 305-0006, Japan
  3. Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA
  4. School of Medicine/School of Dentistry, Surgical Oncology/Oral Biology and Medicine, University of California, Los Angeles, California 90095-1668, USA
  5. Department of Molecular Genetics, Beckman Research Institute of the City of Hope, 1450 East Duarte, Duarte, California 91010, USA
  6. Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Tokyo 113-8656, Japan
  7. Present address: Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.

Correspondence to: Kazunari K. Yokoyama1 Correspondence and requests for materials should be addressed to K.K.Y. (e-mail: Email: kazunari@rtc.riken.go.jp).

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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.