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Molecular and Cellular Biology, April 2004, p. 3473-3484, Vol. 24, No. 8
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.8.3473-3484.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Repression of PML Nuclear Body-Associated Transcription by Oxidative Stress-Activated Bach2

Satoshi Tashiro,1* Akihiko Muto,1 Keiji Tanimoto,1,{dagger} Haruka Tsuchiya,1 Hiroshi Suzuki,1 Hideto Hoshino,2,3,{ddagger} Minoru Yoshida,3,4 Joachim Walter,1,§ and Kazuhiko Igarashi1,3*

Department of Biomedical Chemistry and Leukemia Program Project, Hiroshima University Graduate School of Biomedical Sciences, Hiroshima 734-8551,1 Department of Biotechnology, The University of Tokyo, Tokyo 113-8657,2 Chemical Genetics Laboratory, RIKEN, Wako, Saitama 351-0198,4 CREST Research Project, Japan Science and Technology Agency, Saitama 332-0012, Japan3

Received 29 September 2003/ Returned for modification 25 November 2003/ Accepted 21 January 2004

Several lines of evidence suggest that gene expression is regulated not only by the interaction between transcription factors and DNA but also by the higher-order architecture of the cell nucleus. PML bodies are one of the most prominent nuclear substructures which have been implicated in transcription regulation during apoptosis and stress responses. Bach2 is a member of the BTB-basic region leucine zipper factor family and represses transcription activity directed by the 12-O-tetradecanoylphorbol-13-acetate response element, the Maf recognition element, and the antioxidant-responsive element. Bach2 forms nuclear foci associated with PML bodies upon oxidative stress. Here, we demonstrate that transcription activity associated with PML bodies is selectively repressed by the recruitment of Bach2 around PML bodies. Fluorescence recovery after photobleaching experiments revealed that Bach2 showed rapid turnover in the nuclear foci. The Bach2 N-terminal region including the BTB domain is essential for the focus formation. Sumoylation of Bach2 is required for the recruitment of the protein around PML bodies. These observations represent the first example of modulation of transcription activity associated with PML bodies by a sequence-specific transcription factor upon oxidative stress.

* Corresponding author. Mailing address: Department of Biomedical Chemistry, Hiroshima University Graduate School of Biomedical Sciences, Kasumi 1-2-3, Minamiku, Hiroshima 734-8551, Japan. Phone: 81-82-257-5136. Fax: 81-82-257-5139. E-mail for Satoshi Tashiro: ktashiro{at}hiroshima-u.ac.jp. E-mail for Kazuhiko Igarashi: igarak{at}hiroshima-u.ac.jp.

{dagger} Present address: Department of Translational Cancer Research, Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima 734-8551, Japan.

{ddagger} Present address: Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Higashi, Tsukuba, Ibaraki 305-8566, Japan.

§ Present address: Till I.D., 82152 Martinsried, Germany.

Molecular and Cellular Biology, April 2004, p. 3473-3484, Vol. 24, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.8.3473-3484.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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