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

被引：4

作者：

Reddi, HV ^{[1
]}

Kumar, V ^{[1
]}

机构：

[1] Int Ctr Genet Engn & Biotechnol, Virol Grp, New Delhi 110067, India

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 317卷 / 04期

关键词：

beta-galactosidase; 3AT; HBx; dimerization; yeast two-hybrid; protein-protein interaction;

D O I：

10.1016/j.bbrc.2004.03.140

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 H13x (X0) and its truncated mutants (X15 and X16) were constructed by separately ligating the DNA-binding (BD) and transactivation domains (AD) of Ga14. Co-transformants of the BD and AD constructs of H13x 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 H13x 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. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：1017 / 1022

页数：6

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