REPAIRtoire - a database of DNA repair pathways

Welcome! Click here to login or here to register.
Home
Proteins
DNA damage
Diseases
Homologs
Pathways
Keywords
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

"Hepatitis B virus X protein interferes with cell viability through interaction with the p127-kDa UV-damaged DNA-binding protein."

Lin-Marq N, Bontron S, Leupin O, Strubin M



Published Sept. 1, 2001 in Virology volume 287 .

Pubmed ID: 11531405

Abstract:
The hepatitis B virus X protein (HBx) is essential for establishing natural viral infection and has been implicated in the development of liver cancer associated with chronic infection. The basis for HBx function in either process is not understood. In cell culture, HBx exhibits pleiotropic activities affecting transcription, DNA repair, cell growth, and apoptotic cell death. Numerous cellular proteins including the p127-kDa subunit of UV-damaged DNA-binding activity have been reported to interact with HBx but the functional significance of these interactions remains unclear. Here we show that the binding of HBx to p127 interferes with cell viability. Mutational analysis reveals that HBx contacts p127 via a region to which no function has been assigned previously. An HBx variant bearing a single-charge reversal substitution within this region loses p127 binding and concomitant cytotoxicity. This mutant regains activity when directly fused to p127. These studies confirm that p127 is an important cellular target of HBx, and they indicate that HBx does not exert its effect by sequestering p127, and thereby preventing its normal function, but instead by conferring to p127 a deleterious activity.


This publication refers to following REPAIRtoire entries:

Proteins


Last modification of this entry: Oct. 6, 2010

Add your own comment!

There is no comment yet.
Welcome stranger! Click here to login or here to register.
Valid HTML 4.01! This site is Emacs powered. Made with Django.