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The carboxy‐terminus of the hepatitis B virus X protein is necessary and sufficient for the activation of hypoxia‐inducible factor‐1α
Author(s) -
Yoo Young-Gun,
Cho Sayeon,
Park Sun,
Lee Mi-Ock
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.004
Subject(s) - hbx , transactivation , hypoxia inducible factor 1 , hypoxia inducible factors , transcription factor , hepatitis b virus , chemistry , biology , basic helix loop helix , microbiology and biotechnology , virus , dna binding protein , virology , biochemistry , gene
Hepatitis B virus X protein (HBx) of the hepatitis B virus is strongly implicated in angiogenesis and metastasis during hepatocarcinogenesis. Previously, we reported that HBx enhances activity of hypoxia‐inducible factor‐1α (HIF‐1α), a potent transactivator that induces angiogenic factors. Here, we delineate the structural region of HBx that potentiates HIF‐1α. The carboxy‐terminus of HBx increased the stability of HIF‐1α protein, probably through inhibiting interaction with von Hippel‐Lindau protein. Further, the carboxy‐terminus of HBx enhanced the transactivation function of HIF‐1α by enhancing its association with CREB binding protein (CBP). Finally, we demonstrated the physical association of HBx with the basic helix–loop–helix/PER–ARNT–SIM domain, the inhibitory domain, and the carboxy‐terminal transactivation domain of HIF‐1α in vivo.