THE HEPATITIS-B VIRUS-ENCODED TRANSCRIPTIONAL TRANSACTIVATOR HBX APPEARS TO BE A NOVEL PROTEIN SERINE THREONINE KINASE

被引：120

作者：

WU, JY ^{[1
]}

ZHOU, ZY ^{[1
]}

JUDD, A ^{[1
]}

CARTWRIGHT, CA ^{[1
]}

ROBINSON, WS ^{[1
]}

机构：

[1] SRI INT,MENLO PK,CA 94025

来源：

CELL | 1990年 / 63卷 / 04期

关键词：

D O I：

10.1016/0092-8674(90)90135-2

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：

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. © 1990.

引用

页码：687 / 695

页数：9

共 52 条

[1] PROTEIN-KINASE ACTIVITY IN HEPATITIS-B VIRUS [J].