RRC ID 42152
Author Tanaka Y, Kanai F, Kawakami T, Tateishi K, Ijichi H, Kawabe T, Arakawa Y, Kawakami T, Nishimura T, Shirakata Y, Koike K, Omata M.
Title Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis.
Journal Biochem Biophys Res Commun
Abstract Understanding the function of the hepatitis B virus X protein (HBx) is fundamental to elucidating the underlying mechanisms of hepatitis and hepatocarcinogenesis caused by hepatitis B virus (HBV) infection. We identified heat shock protein 60 (Hsp60) as a novel cellular target of HBx by the combination of affinity purification and mass spectrometry. Physical interaction between HBx and Hsp60 was confirmed by standard immunoprecipitation and immunoblot methods. Analysis of HBx deletion constructs showed that amino acids 88-117 of HBx were responsible for the binding to Hsp60. Confocal laser microscopy demonstrated that HBx and Hsp60 colocalized in mitochondria. Furthermore, terminal deoxynucleotidyl transferase-mediated dUTP end labeling (TUNEL) revealed that the introduction of Hsp60 into cells facilitated HBx-induced apoptosis. These findings suggest the importance of the molecular chaperon protein Hsp60 to the function of HBV viral proteins.
Volume 318(2)
Pages 461-9
Published 2004-5-28
DOI 10.1016/j.bbrc.2004.04.046
PII S0006291X04007673
PMID 15120623
MeSH Amino Acid Sequence Apoptosis / physiology* Cell Line Chaperonin 60 / genetics Chaperonin 60 / metabolism* Chromatography, Affinity Hepatocytes / cytology Hepatocytes / metabolism Humans Immunoblotting Immunohistochemistry In Situ Nick-End Labeling Mass Spectrometry Mitochondria / metabolism Molecular Sequence Data Precipitin Tests Protein Binding Recombinant Proteins / genetics Recombinant Proteins / metabolism Sequence Analysis, Protein / methods Sequence Deletion Trans-Activators / metabolism* Trans-Activators / physiology Transfection Viral Regulatory and Accessory Proteins
IF 2.985
Times Cited 63
Human and Animal Cells HuH-7(RCB1366)