Self-association of the hepatitis B virus X protein in the yeast two-hybrid system. Biochem Biophys Res Commun 2004 May 14;317(4):1017-22
Date
04/20/2004Pubmed ID
15094370DOI
10.1016/j.bbrc.2004.03.140Scopus ID
2-s2.0-1942516396 (requires institutional sign-in at Scopus site) 3 CitationsAbstract
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.
Author List
Reddi HV, Kumar VMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceBase Sequence
Genetic Vectors
Molecular Sequence Data
Recombinant Fusion Proteins
Templates, Genetic
Trans-Activators
Transformation, Genetic
Two-Hybrid System Techniques
Viral Regulatory and Accessory Proteins
Yeasts
beta-Galactosidase
