Biochemical Characterization of Recombinant Hepatitis C Virus Nonstructural Protein 4B: Evidence for ATP/GTP Hydrolysis and Adenylate Kinase Activity†

Biochemistry ◽  
2009 ◽  
Vol 48 (5) ◽  
pp. 906-916 ◽  
Author(s):  
Aaron A. Thompson ◽  
Aihua Zou ◽  
Jiangli Yan ◽  
Rohit Duggal ◽  
Weidong Hao ◽  
...  
2013 ◽  
Vol 87 (19) ◽  
pp. 10612-10627 ◽  
Author(s):  
D. Paul ◽  
S. Hoppe ◽  
G. Saher ◽  
J. Krijnse-Locker ◽  
R. Bartenschlager

Marine Drugs ◽  
2014 ◽  
Vol 12 (1) ◽  
pp. 462-476 ◽  
Author(s):  
Atsushi Furuta ◽  
Kazi Salam ◽  
Idam Hermawan ◽  
Nobuyoshi Akimitsu ◽  
Junichi Tanaka ◽  
...  

2011 ◽  
Vol 156 (9) ◽  
pp. 1591-1601 ◽  
Author(s):  
Koji Yokoyama ◽  
Masaharu Takahashi ◽  
Tsutomu Nishizawa ◽  
Shigeo Nagashima ◽  
Suljid Jirintai ◽  
...  

Gene ◽  
1996 ◽  
Vol 182 (1-2) ◽  
pp. 203-211 ◽  
Author(s):  
Yoshihiro Ide ◽  
Luwen Zhang ◽  
Min Chen ◽  
Genevieve Inchauspe ◽  
Chander Bahl ◽  
...  

1997 ◽  
Vol 34 (2) ◽  
pp. A93
Author(s):  
CH Hagedorn ◽  
RH Al ◽  
C De Staercke ◽  
Y Wang ◽  
Y Xie

2005 ◽  
Vol 79 (12) ◽  
pp. 7911-7917 ◽  
Author(s):  
Rainer Gosert ◽  
Wiebke Jendrsczok ◽  
Jan Martin Berke ◽  
Volker Brass ◽  
Hubert E. Blum ◽  
...  

ABSTRACT Protein-protein interactions involved in formation of the membrane-associated hepatitis C virus (HCV) replication complex are poorly understood. Here, we investigated nonstructural proteins with deletions in their membrane anchor domains when expressed in the context of the entire HCV polyprotein. Interactions among cytosolic domains of HCV nonstructural proteins were found not to be sufficiently strong to rescue such mutants to the membrane. Thus, the membrane anchor domains of nonstructural proteins are essential for incorporation of these proteins into the HCV replication complex while interactions among the cytosolic domains appear to be relatively weak. This feature may provide the nonstructural proteins with a certain flexibility to perform their multiple functions during HCV replication.


2004 ◽  
Vol 78 (18) ◽  
pp. 10202-10205 ◽  
Author(s):  
Guang Yang ◽  
Daniel C. Pevear ◽  
Marc S. Collett ◽  
Srinivas Chunduru ◽  
Dorothy C. Young ◽  
...  

ABSTRACT Biochemical characterization of hepatitis C virus (HCV) replication using purified, membrane-associated replication complexes is hampered by the presence of endogenous nuclease activity that copurifies with the replication complex. In this study, pulse-chase analyses were used to demonstrate that newly synthesized replicon RNA was protected from nuclease activity by a factor(s) that was sensitive to 0.5% NP-40 or protease treatment. Nuclease susceptibility was not related to disruption of lipid membranes, since NP-40 did not significantly affect the buoyant density of HCV replication complexes or protease susceptibility of HCV NS3 and NS5A proteins. These results suggest that a protease-sensitive factor(s) protects newly synthesized RNA from nuclease degradation.


2000 ◽  
Vol 267 (12) ◽  
pp. 3685-3694 ◽  
Author(s):  
Kotaro Fukuda ◽  
Daesety Vishnuvardhan ◽  
Satoru Sekiya ◽  
Joonsung Hwang ◽  
Nobuko Kakiuchi ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document