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(Received for publication, October 11, 1996, and in revised form, January 3, 1997)
From the Department of Molecular Biology, Cancer Research
Institute, Kanazawa University, Takara-machi 13-1, Kanazawa 920, Japan
Hepatitis B virus X protein (HBx) transactivates
viral and cellular genes through a wide variety of
cis-elements. However, the mechanism is still obscure. Our
finding that HBx directly interacts with RNA polymerase II subunit 5 (RPB5), a common subunit of RNA polymerases, implies that HBx directly
modulates the function of RNA polymerase (Cheong, J. H., Yi, M., Lin,
Y., and Murakami, S. (1995) EMBO J. 14, 142-150). In this
context, we examined the possibility that HBx and RPB5 interact with
other general transcription factors. HBx and RPB5 specifically bound to
transcription factor IIB (TFIIB) in vitro, both of which
were detected by either far-Western blotting or the glutathione
S-transferase-resin pull-down assay. Delineation of the
binding regions of these three proteins revealed that HBx, RPB5, and
TFIIB each has two binding regions for the other two proteins.
Co-immunoprecipitation using HepG2 cell lysates that express HBx
demonstrated trimeric interaction in vivo. Some HBx
substitution mutants, which had severely impaired transacting activity,
exhibited reduced binding affinity with either TFIIB or RPB5 in a
mutually exclusive manner, suggesting that HBx transactivation requires
the interactions of both RPB5 and TFIIB. These results indicated that
HBx is a novel virus modulator that facilitates transcriptional
initiation by stabilizing the association between RNA polymerase and
TFIIB through communication with RPB5 and TFIIB.
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