Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins
SCIE
SCOPUS
- Title
- Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins
- Authors
- Goo, YH; Sohn, YC; Kim, DH; Kim, SW; Kang, MJ; Jung, DJ; Kwak, E; Barlev, NA; Berger, SL; Chow, VT; Roeder, RG; Azorsa, DO; Meltzer, PS; Suh, PG; Song, EJ; Lee, KJ; Lee, YC; Lee, JW
- Date Issued
- 2003-01
- Publisher
- AMER SOC MICROBIOLOGY
- Abstract
- 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/beta-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 methyllation 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/11680
- DOI
- 10.1128/MCB.23.1.140
- ISSN
- 0270-7306
- Article Type
- Article
- Citation
- MOLECULAR AND CELLULAR BIOLOGY, vol. 23, no. 1, page. 140 - 149, 2003-01
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