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RISS 인기검색어
- 검색키워드
- 저자 : Nickolai A. Barlev (검색결과 2 건)
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Goo, Young-Hwa,Sohn, Young Chang,Kim, Dae-Hwan,Kim, Seung-Whan,Kang, Min-Jung,Jung, Dong-Ju,Kwak, Eunyee,Barlev, Nickolai A.,Berger, Shelley L.,Chow, Vincent T.,Roeder, Rober G.,Azora, David O.,Meltze 梨花女子大學校 藥學硏究所 2003 藥學硏究論文集 Vol.- No.12
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, α/β-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-lysjne 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.
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Sohn, Young Chang,Goo, Young-Wha,Kim, Dae-Hwan,Kim, Seung-Whan,Kang, Min-Jung,Nickolai A. Barlev,Shelley L. Berger,Vincent T. Chow,Suh, Pan-Gil,David O. Azorsa,Paul S. Meltzer,Lee, Kong-Ju,Lee, Young- 이화여자대학교 세포신호전달연구센터 2002 고사리 세포신호전달 심포지움 Vol. No.4
Activating signal cointegrator-2(ASC-2), also reported as AIB3, TRBP, RAP250, NRC and PRIP, directly binds to and functions as a coactivator molecule of nuclear receptors and many other transcription factors. In particular, our previous results from microinjection of anti-ASC2 antibody demonstrated that ASC-2 is required for transactivation by nuclear receptors and AP-1 in vivo. Here we show that ASC-2 belongs to a steady-state complex of approximately 2 MDa(ASCOM for ASC-2 complex) in HeLa nuclei, which contains mammalian homologues of Drosophila Trithorax group(Trx-G) proteins ALR-1, ALR-2, HALR and ASH2. ALR-1/2 and HALR contain a SET domain that specifically methylates histone H3 lysine 4(K4). We further demonstrate that retinoic acid receptor(RAR) transactivation requires retinoid-dependent recruitment of ASCOM to DNA-bound RAR in vivo. Thus, ASCOM represents the first mammalian coactivator complex with H3/K4-methylase activity, directly recruited to nuclear receptors.
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