Self-association of the hepatitis B virus X protein in the yeast two-hybrid system.
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.
Reddi
Honey V
HV
Virology Group, International Centre for Genetic Engineering and Biotechnology, P.O. Box 10504, Aruna Asaf Ali Marg, New Delhi-110067, India.
Kumar
Vijay
V
D000595:Amino Acid Sequence; D001483:Base Sequence; D005822:Genetic Vectors; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013698:Templates, Genetic; D015534:Trans-Activators / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014170:Transformation, Genetic; D020798:Two-Hybrid System Techniques; D054334:Viral Regulatory and Accessory Proteins; D015003:Yeasts / Q000235:genetics* / Q000254:growth & development; D001616:beta-Galactosidase / Q000378:metabolism
D011993:Recombinant Fusion Proteins; D015534:Trans-Activators; D054334:Viral Regulatory and Accessory Proteins; C057628:hepatitis B virus X protein; D001616:beta-Galactosidase