Molecular cloning of the rabbit interleukin 6 promoter: Functional characterization of rabbit hemorrhagic disease virus response elements in RK-13 cells

2016 ◽  
Vol 65 ◽  
pp. 280-288 ◽  
Author(s):  
Xing Liu ◽  
Bo Hu ◽  
Fang Wang ◽  
Yanhua Song ◽  
Zhiyu Fan ◽  
...  
2000 ◽  
Vol 74 (22) ◽  
pp. 10846-10851 ◽  
Author(s):  
M. Soledad Marín ◽  
Rosa Casais ◽  
José M. Martín Alonso ◽  
Francisco Parra

ABSTRACT The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 polyprotein cleavage product has been expressed inEscherichia coli as a glutathione S-transferase (GST) fusion protein. The recombinant GST-Δ2C protein showed in vitro ATP-binding and ATPase activities. Site-directed mutagenesis studies of the conserved residues G522 and T529 in motif A, D566 and E567 in motif B, and K600 in motif C were also performed. These results provide the first experimental characterization of a 2C-like ATPase activity in a member of the Caliciviridae.


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