Artículos de revistas
Expression Of Deletion Mutants Of The Hepatitis B Virus Protein Hbx In E. Coli And Characterization Of Their Rna Binding Activities
Registro en:
Virus Research. , v. 74, n. 1-2, p. 59 - 73, 2001.
1681702
10.1016/S0168-1702(00)00245-8
2-s2.0-0035114391
Autor
Rui E.
De Moura P.R.
Kobarg J.
Institución
Resumen
The hepatitis B virus protein HBx has been implicated in the development of liver cancer. It has been shown that the HBx protein is able to bind to single-stranded DNA in a specific manner. This DNA binding activity might be relevant for HBx oncogene character. To study the HBx interaction with nucleic acids in more detail we expressed full-length HBx as well as several N- and C-terminally truncated HBx proteins as 6xHis and GST-fusions in E. coli. Using a gel shift assay, we were able to demonstrate that all of the truncated HBx proteins have the ability to bind to an AU-rich RNA. The affinity of GST-HBx #3 (residues 80-142) was an order of magnitude higher than that of GST-HBx #2 (residues 5-79), indicating that a high affinity RNA binding site is located in HBx C-terminal half. AUF1 is the protein ligand that binds to AU-rich RNA regions present in certain proto-oncogene mRNAs and causes their rapid degradation. 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