Direct binding of hepatitis B virus X protein and retinoid X receptor contributes to phosphoenolpyruvate carboxykinase gene transactivation

FEBS Letters

Lee, Jae Woon¹  Cheong, JaeHun¹  Kong, Hee Jeong¹  Lee, Min Young¹  Kim, Han Do²  Hong, Sun Hwa¹ 

[1] Center for Ligand and Transcription, Chonnam National University, Kwangju 500-757, South Korea;Department of Molecular Biology, Pusan National University, Pusan 609-735, South Korea

关键词: Hepatitis B virus X protein;    Phosphoenolpyruvate carboxykinase;    Retinoid X receptor;    ATF-2;    Transactivation;    HBV;    hepatitis B virus;    PEPCK;    phosphoenolpyruvate carboxykinase;    HBx;    hepatitis B virus X protein;    CRE;    cAMP response element;    RAR;    retinoic acid receptor;    RXR;    retinoid X receptor;    GR;    glucocorticoid receptor;    TR;    thyroid hormone receptor;    LBD;    ligand binding domain;    GST;    glutathione S-transferase;   

DOI  :  10.1016/S0014-5793(00)02091-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The X gene product of the human hepatitis B virus (HBx), a major factor responsible for hepatitis and hepatocellular carcinoma, modulates transactivation by a variety of transcription factors. Herein, expression of the phosphoenolpyruvate carboxykinase (PEPCK) gene was found to be regulated transcriptionally by HBx through two distinct promoter regions. The cAMP response element (CRE)-1 site within the proximal promoter region mediated the HBx-induced transactivation of the PEPCK gene through C/EBPα and ATF-2. A retinoid X receptor (RXR) response element within the distal promoter region also contributed to the HBx-induced transactivation. Consistent with these results, HBx directly interacted with RXR, and the interaction interfaces were localized to the transactivation domain of HBx and the ligand binding domain of RXR.

【 授权许可】

Unknown