Role of glyceraldehyde-3-phosphate dehydrogenase binding to hepatitis B virus posttranscriptional regulatory element in regulating expression of HBV surface antigen

2009 ◽  
Vol 154 (3) ◽  
pp. 519-524 ◽  
Author(s):  
Yi Li ◽  
Tingting Huang ◽  
Xiaohua Zhang ◽  
Tao Wan ◽  
Jieli Hu ◽  
...  
1998 ◽  
Vol 72 (6) ◽  
pp. 5085-5092 ◽  
Author(s):  
John E. Donello ◽  
Jonathan E. Loeb ◽  
Thomas J. Hope

ABSTRACT The hepatitis B virus posttranscriptional regulatory element (HBVPRE) is a cis-acting RNA element that partially overlaps with enhancer I and is required for the cytoplasmic accumulation of HBV surface RNAs. We find that the closely related woodchuck hepatitis virus (WHV), which has been shown to lack a functional enhancer I, also contains a posttranscriptional regulatory element (WPRE). Deletion analysis suggests that the WPRE consists of three independent subelements. Comparison of the bipartite HBVPRE and tripartite WPRE activities reveals that the tripartite WPRE is two to three times more active than the bipartite HBVPRE. Mutation of a single WPRE subelement decreases WPRE activity to the level of the HBVPRE. Bipartite and tripartite chimeras of the WPRE and HBVPRE possess activities which suggest that elements containing three subelements are posttranscriptionally stronger than those containing two. These data demonstrate that the posttranscriptional regulatory element is conserved within the mammalian hepadnaviruses and that its strength is determined by the number of subelements within the RNA.


1996 ◽  
Vol 70 (7) ◽  
pp. 4345-4351 ◽  
Author(s):  
J E Donello ◽  
A A Beeche ◽  
G J Smith ◽  
G R Lucero ◽  
T J Hope

2001 ◽  
Vol 75 (22) ◽  
pp. 10779-10786 ◽  
Author(s):  
Wei-Qing Zang ◽  
Bin Li ◽  
Pei-Yong Huang ◽  
Michael M. C. Lai ◽  
T. S. Benedict Yen

ABSTRACT The hepatitis B virus posttranscriptional regulatory element (PRE) is an RNA element that increases the expression of unspliced mRNAs, apparently by facilitating their export from the nucleus. We have identified a cellular protein that binds to the PRE as the polypyrimidine tract binding protein (PTB), which shuttles rapidly between the nucleus and the cytoplasm. Mutants of the PRE with mutations in PTB binding sites show markedly decreased activity, while cells that stably overexpress PTB show increased PRE-dependent gene expression. Export of PTB from the nucleus, like PRE function, is blocked by a mutant form of Ran binding protein 1 but not by leptomycin B. Therefore, PTB is important for PRE activity and appears to function as an export factor for PRE-containing mRNAs.


2005 ◽  
Vol 11 (8) ◽  
pp. 922-928 ◽  
Author(s):  
Alessandro Franchello ◽  
Valeria Ghisetti ◽  
Alfredo Marzano ◽  
Renato Romagnoli ◽  
Mauro Salizzoni

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