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J Biol Chem, Vol. 273, Issue 42, 27097-27103, October 16, 1998

The Hepatitis B Virus X Protein Is a Co-activator of Activated Transcription That Modulates the Transcription Machinery and Distal Binding Activators

Yong Lin, Hong Tang, Takahiro Nomura, Dorjbal Dorjsuren, Naoyuki Hayashi, Wenxiang Wei, Tsutomu Ohta, Robert Roeder^§, and Seishi Murakami

From the Department of Molecular Biology, Cancer Research Institute, Kanazawa University, Takara-machi 13-1, Kanazawa 920-0934, Japan,  National Institute of Genetics, Mishima 411-0801, Japan, and ^§ Rockefeller University, New York, New York 10021

Hepatitis B virus X protein (HBx) transactivates viral and cellular genes through a wide variety of cis-elements, but the mechanism has not been well elucidated. Evidence for nuclear events in HBx transactivation has been reported. Here we examine the role of HBx in modulation of transcription with a transient transfection system and an in vitro transcription assay. Reporters bearing Gal4-binding sites were applied to avoid the effects of endogenous transcription factors with or without signaling processes. The Gal4-DNA binding domain fused form of HBx exhibited no effect on Gal4-responsive reporters. However, HBx augmented activated transcription by transcriptional activators, suggesting HBx retains a co-activator but not a transcriptional activator function. The functional domain for co-activation was the same as that for HBx transactivation, and the transcription factor IIB- and RNA polymerase II subunit 5-interacting sites of HBx, which were critical for HBx transactivation, were shown to be crucial for the co-activation function. Importantly, HBx stimulated transcription on templates bearing the X responsive elements in vitro with endogenous activators. These results imply that HBx acts as a co-activator that modulates transcriptional machinery and distal-binding activators, which may explain one of the mechanisms of transactivation by HBx when localized in nuclei.

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