Publication date: Available online 14 November 2016 Source:Biochemical and Biophysical Research Communications
Author(s): Ae-Ree Lee, Yeo-Jin Seo, Seo-Ree Choi, Kyoung-Seok Ryu, Hae-Kap Cheong, Shim Sung Lee, Chin-Ju Park, Joon-Hwa Lee
A Z-DNA binding protein (ZBP)-containing protein kinase (PKZ) in fish species has an important role in the innate immune response. Previous structural studies of the Z? domain of the PKZ from Carassius auratus (caZ?PKZ) showed that the protein initially binds to B-DNA and induces B-Z transition of double stranded DNA in a salt concentration-dependent manner. However, the significantly reduced B-Z transition activity of caZ?PKZ at high salt concentration was not fully understood. In this study, we present the binding affinity of the protein for B-DNA and Z-DNA and characterize its extremely low B-Z transition activity at 250*mM NaCl. Our results emphasize that the B-DNA-bound form of caZ?PKZ can be used as molecular ruler to measure the degree of B-Z transition.
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Linear Mode
