Figure - PMC

Skip to main content

View full-text article in PMC

. Author manuscript; available in PMC: 2013 Jun 1.

Published in final edited form as: Hepatology. 2012 Jan 30;55(6):1662–1672. doi: 10.1002/hep.25533

Fig. 2 — The C-terminal region of NS5A domain I is necessary and sufficient for its interaction with the nucleotide binding domain of HSP70. The upper part of all panels displays Western analysis of GST pull-down targets using antibody against the V5 epitope. Arrows indicate presence of target polypeptides. The lower part(s) represent(s) Coomassie stains showing GST-fusion bait proteins. (A) The N-terminal region of NS5A domain I is not necessary for HSP70 binding. (B) The C-terminal 34 amino acids of NS5A domain I (C34) are necessary for HSP70 interaction. (C) C34 region is sufficient for HSP70 binding. (D) Schematic of the structure of NS5A. (E) Summary of all NS5A subclones used in GST pull-down analyses in Fig. 1 and 2. (+) and (−) indicate interaction and lack of interaction with HSP70, respectively. (F) NS5A domain I directly interacts with the nucleotide binding domain of HSP70, but not with the substrate binding domain.

Fig. 2 — The C-terminal region of NS5A domain I is necessary and sufficient for its interaction with the nucleotide binding domain of HSP70. The upper part of all panels displays Western analysis of GST pull-down targets using antibody against the V5 epitope. Arrows indicate presence of target polypeptides. The lower part(s) represent(s) Coomassie stains showing GST-fusion bait proteins. (A) The N-terminal region of NS5A domain I is not necessary for HSP70 binding. (B) The C-terminal 34 amino acids of NS5A domain I (C34) are necessary for HSP70 interaction. (C) C34 region is sufficient for HSP70 binding. (D) Schematic of the structure of NS5A. (E) Summary of all NS5A subclones used in GST pull-down analyses in Fig. 1 and 2. (+) and (−) indicate interaction and lack of interaction with HSP70, respectively. (F) NS5A domain I directly interacts with the nucleotide binding domain of HSP70, but not with the substrate binding domain.