1. Physical interaction between hepatitis C virus NS4B protein and CREB-RP/ATF6β
- Author
-
Yuki Takigawa, Lin Deng, Rachmat Hidajat, Motoko Nagano-Fujii, Wen Yan Tong, and Hak Hotta
- Subjects
Macromolecular Substances ,viruses ,Molecular Sequence Data ,Biophysics ,Activating transcription factor ,Biology ,Viral Nonstructural Proteins ,CREB ,Biochemistry ,Protein–protein interaction ,Fungal Proteins ,Two-Hybrid System Techniques ,Yeasts ,Humans ,Amino Acid Sequence ,Molecular Biology ,Transcription factor ,ATF3 ,Leucine Zippers ,Endoplasmic reticulum ,bZIP domain ,Cell Biology ,Molecular biology ,Activating Transcription Factor 6 ,Protein Structure, Tertiary ,DNA-Binding Proteins ,Microscopy, Fluorescence ,Unfolded protein response ,biology.protein ,HeLa Cells ,Protein Binding ,Transcription Factors - Abstract
By using a yeast two-hybrid assay, cyclic AMP-response-element-binding protein-related protein (CREB-RP), also called activating transcription factor 6beta (ATF6beta), was identified as a cellular protein that interacts with the NS4B protein of hepatitis C virus. An N-terminal half of NS4B and a central portion of CREB-RP/ATF6beta containing the basic leucine zipper (bZIP) domain were involved in the interaction. The interaction between NS4B and CREB-RP/ATF6beta was demonstrated also in mammalian cells by co-immunoprecipitation and confocal microscopic analyses using specific antibodies. The bZIP domain of ATF6alpha, which shares high sequence similarity with CREB-RP/ATF6beta, was also shown to interact with NS4B in yeast although the interaction was weaker than that between NS4B and CREB-RP/ATF6beta. CREB-RP/ATF6beta and ATF6alpha are known as endoplasmic reticulum (ER) stress-induced transcription factors. Collectively, our results imply the possibility that NS4B modulates certain cellular responses upon ER stress through the physical interaction with CREB-RP/ATF6beta and ATF6alpha.
- Published
- 2002