The hepatitis B virus-encoded transcriptional trans-activator hbx appears to be a novel protein serine/threonine kinase

Jane Y. Wu*, Zhuo Yuan Zhou, Amrit Judd, Christine A. Cartwright, William S. Robinson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

86 Scopus citations

Abstract

To study the functional mechanism of the hepatitis B virus (HBV) X (hbx) gene product, we have expressed the hbx protein in E. coli and purified it by HPLC. The purified hbx protein was shown to be active in trans-activating transcription directed by the LTR sequence of HIV-1. The hbx protein was found to have an intrinsic serine/threonine protein kinase activity. The hbx protein was detected in hepatitis B virions, and tryptic phosphopeptide maps of the hbx protein phosphorylated in the virion and of the in vitro phosphorylated bacterially expressed hbx protein were similar. Inactivation of the hbx protein by heat, protein-denaturing agents, or an ATP affinity analog, p-fluorosulfonyl-benzoyl 5′-adenosine, resulted in loss of both protein kinase activity and trans-activation activity. These results suggest that the HBV-encoded trans-activator hbx is a novel protein kinase.

Original languageEnglish (US)
Pages (from-to)687-695
Number of pages9
JournalCell
Volume63
Issue number4
DOIs
StatePublished - Nov 16 1990

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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