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

  • Hee Jeong Kong
  • , Sun Hwa Hong
  • , Min Young Lee
  • , Han Do Kim
  • , Jae Woon Lee
  • , Jae Hun Cheong

Research output: Contribution to journalArticlepeer-review

Abstract

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. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)114-118
Number of pages5
JournalFEBS Letters
Volume483
Issue number2-3
DOIs
StatePublished - Oct 20 2000
Externally publishedYes

Funding

We thank Dr. Seishi Murakami for the HBx expression constructs. This research was exclusively supported by the National Creative Research Initiatives Program of the Korean Ministry of Science and Technology (awarded to J.W.L.).

Funders
Ministry of Education, Science and Technology

    Keywords

    • ATF-2
    • Hepatitis B virus X protein
    • Phosphoenolpyruvate carboxykinase
    • Retinoid X receptor
    • Transactivation

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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