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Self-association of the hepatitis B virus X protein in the yeast two-hybrid system.

Abstract：

:Self-association of the transactivator HBx protein of hepatitis B virus was investigated using the yeast two-hybrid system. Expression vectors for the full-length HBx (X0) and its truncated mutants (X15 and X16) were constructed by separately ligating the DNA-binding (BD) and transactivation domains (AD) of Gal4. Co-transformants of the BD and AD constructs of HBx were selected using defined minimal medium and analyzed for the reconstitution of beta-galactosidase activity. No two-hybrid interaction was observed either between the full-length HBx molecules or its highly truncated mutant X16. However, a strong functional interaction between X0 and X15, X0 and X16, and X15 and X16 suggested that HBx could self-associate in a cellular environment through its carboxy-terminal region.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Reddi HV,Kumar V

doi

10.1016/j.bbrc.2004.03.140

subject

Has Abstract

pub_date

2004-05-14 00:00:00

pages

1017-22

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006291X04006448

journal_volume

317

pub_type

杂志文章

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