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Molecular and Cellular Biology, January 2003, p. 140-149, Vol. 23, No. 1
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.1.140-149.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Activating Signal Cointegrator 2 Belongs to a Novel Steady-State Complex That Contains a Subset of Trithorax Group Proteins

Young-Hwa Goo,1 Young Chang Sohn,2 Dae-Hwan Kim,3 Seung-Whan Kim,1 Min-Jung Kang,1 Dong-Ju Jung,1 Eunyee Kwak,1 Nickolai A. Barlev,4 Shelley L. Berger,4 Vincent T. Chow,5 Robert G. Roeder,6 David O. Azorsa,7 Paul S. Meltzer,7 Pan-Gil Suh,1 Eun Joo Song,8 Kong-Joo Lee,8 Young Chul Lee,3* and Jae Woon Lee1*

Department of Life Science, Pohang University of Science and Technology, Pohang 790-784,1 Division of Marine Life Sciences, Kangnung National University, Kangnung 210-702,2 Hormone Research Center, Chonnam National University, Kwangju 500-757,3 Center for Cell Signaling Research, Division of Molecular Life Sciences and College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea,8 Department of Microbiology, Faculty of Medicine, National University of Singapore, Singapore 117597, Republic of Singapore,5 Molecular Genetics Program, The Wistar Institute, Philadelphia, Pennsylvania 19104,4 Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021,6 Cancer Genetics Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892-44707

Received 1 July 2002/ Returned for modification 21 August 2002/ Accepted 2 October 2002

Many transcription coactivators interact with nuclear receptors in a ligand- and C-terminal transactivation function (AF2)-dependent manner. These include activating signal cointegrator 2 (ASC-2), a recently isolated transcriptional coactivator molecule, which is amplified in human cancers and stimulates transactivation by nuclear receptors and numerous other transcription factors. In this report, we show that ASC-2 belongs to a steady-state complex of approximately 2 MDa (ASC-2 complex [ASCOM]) in HeLa nuclei. ASCOM contains retinoblastoma-binding protein RBQ-3, {alpha}/ß-tubulins, and trithorax group proteins ALR-1, ALR-2, HALR, and ASH2. In particular, ALR-1/2 and HALR contain a highly conserved 130- to 140-amino-acid motif termed the SET domain, which was recently implicated in histone H3 lysine-specific methylation activities. Indeed, recombinant ALR-1, HALR, and immunopurified ASCOM exhibit very weak but specific H3-lysine 4 methylation activities in vitro, and transactivation by retinoic acid receptor appears to involve ligand-dependent recruitment of ASCOM and subsequent transient H3-lysine 4 methylation of the promoter region in vivo. Thus, ASCOM may represent a distinct coactivator complex of nuclear receptors. Further characterization of ASCOM will lead to a better understanding of how nuclear receptors and other transcription factors mediate transcriptional activation.

* Corresponding author. Mailing address for Jae Woon Lee: Dept. of Life Science, Pohang University of Science and Technology, Pohang 790-784, Korea. Phone: 82-54-279-2129. Fax: 82-54-279-8374. E-mail: jaewoon{at}postech.ac.kr. Mailing address for Young Chul Lee: Hormone Research Center, Chonnam National University, Kwangju 500-757, Korea. Phone: 82-62-530-0909. Fax: 82-62-530-0500. E-mail: yclee{at}chonnam.chonnam.ac.kr.

Molecular and Cellular Biology, January 2003, p. 140-149, Vol. 23, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.1.140-149.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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