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Title 

Functional analysis of hepatitis B virus transactivator X : implication of the leucine zipper-like region and C-Terminal seven conserved amino acids in functional regions

Authors 

Young-Hoon KimSeok-Kwon KangYoung Ik Lee

Publisher 

Elsevier

Issue Date 

1993

Citation 

Biochemical and Biophysical Research Communications, vol. 197, no. 2, pp. 894-903

Keywords 

leucine zipper proteintranscription factorvirus proteinarticlehepatitis b virusstructure activity relationamino acid sequencecell linechloramphenicol o-acetyltransferasecloning, molecular

Abstract 

X protein of hepatitis B virus (HBV-X) is a transactivator to a wide variety of viral and cellular transcriptional regulatory elements. Since HBV- X does not act on a common cis-regulatory element of a wide variety of regulatory elements nor does it bind to DNA directly, it has been proposed that HBV-X acts indirectly through protein-protein interactions with other transcription factors or signal transducing pathway. In order to determine the functional domain of HBV-X, we have constructed and analyzed a number of deletion and site specific mutants. Our results showed that leucine zipper- like sequences were found in the C-terminal region of HBV-X and were very important for its transactivating activity. In the analysis of deletion mutants, seven conserved and strong basic amino acids (amino acids 135-141) were essential for the transactivating activity of HBV-X.

ISSN 

0006-291X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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