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NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration
- Authors
- Lee, Ae-Ree; Seo, Yeo-Jin; Choi, Seo-Ree; Ryu, Kyoung-Seok; Cheong, Hae-Kap; Lee, Shim Sung; Katahira, Masato; Park, Chin-Ju; Lee, Joon-Hwa
- Issue Date
- 8-Jan-2017
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- NMR; Z-DNA; Salt effect; Z-DNA binding protein; DNA-protein interaction
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.482, no.2, pp 335 - 340
- Pages
- 6
- Indexed
- SCI
SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 482
- Number
- 2
- Start Page
- 335
- End Page
- 340
- ISSN
- 0006-291X
1090-2104
- Abstract
- 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 alpha domain of the Pia from Carassius auratus (caZ alpha(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 alpha(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 NaCI. Our results emphasize that the B-DNA-bound form of caZ alpha(PKZ) can be used as molecular ruler to measure the degree of B-Z transition. (C) 2016 Elsevier Inc. All rights reserved.
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