Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution

2017 ◽  
Vol 19 (11) ◽  
pp. 7947-7954 ◽  
Author(s):  
Orion Shih ◽  
Yi-Qi Yeh ◽  
Kuei-Fen Liao ◽  
Tai-Ching Sung ◽  
Yun-Wei Chiang ◽  
...  
Keyword(s):  
X Protein ◽  
Linear Oligomerization

Linear oligomerization of ditopic BAX-dimers into tri-dimer helical units then into a rod-like structure, as revealed using integrated ESR/SAXS/MD analyses.

scholarly journals Hepatitis B Virus X Protein and Simian Virus 5 V Protein Exhibit Similar UV-DDB1 Binding Properties To Mediate Distinct Activities

2003 ◽  
Vol 77 (11) ◽  
pp. 6274-6283 ◽  
Author(s):  
Olivier Leupin ◽  
Séverine Bontron ◽  
Michel Strubin
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Simian Virus ◽  
Binding Activity ◽  
X Protein ◽  
Binding Properties ◽  
V Protein ◽  
Dna Binding Activity ◽  
Simian Virus 5 ◽  
B Virus

ABSTRACT The UV-damaged DNA-binding activity protein (UV-DDB) consists of two subunits, DDB1 and DDB2, and functions in DNA repair and cell cycle regulation. The DDB1 subunit is a target for the hepatitis B virus X protein (HBx). Binding of HBx to DDB1 interferes with cell growth and viability in culture and has been implicated in the establishment of viral infection. DDB1 also interacts with the V proteins encoded by several paramyxoviruses including simian virus 5 (SV5), which prevent interferon signaling by targeting either STAT1 or STAT2 proteins for proteolysis. The role of V binding to DDB1, however, remains unclear. Here we show that the V protein of SV5 (SV5-V) and HBx exhibit strikingly similar DDB1 binding properties. Thus, SV5-V and HBx bind to DDB1 in a mutually exclusive manner, and SV5-V shares with HBx the ability to enhance the steady-state levels of DDB1 and to inhibit its association with DDB2. Yet only HBx induces cell death, and SV5-V can prevent HBx from doing so by blocking its interaction with DDB1. Binding of SV5-V to DDB1 may serve another function, since SV5-V shows a decreased ability to induce STAT1 degradation in cells expressing reduced amounts of DDB1. These findings demonstrate that HBx performs a unique function through its association with DDB1 for which SV5-V cannot substitute and suggest that SV5-V and HBx have evolved to bind DDB1 to achieve distinct functions, both by a mechanism that does not involve DDB2.

scholarly journals Hepatitis B x Protein Inhibits p53-dependent DNA Repair in Primary Mouse Hepatocytes

1998 ◽  
Vol 273 (50) ◽  
pp. 33327-33332 ◽  
Author(s):  
Sandrine Prost ◽  
James M. Ford ◽  
Clare Taylor ◽  
Jennifer Doig ◽  
David J. Harrison
Keyword(s):  
Dna Repair ◽  
Hepatitis B ◽  
X Protein ◽  
Primary Mouse Hepatocytes ◽  
Primary Mouse ◽  
Mouse Hepatocytes
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