title: NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration.
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 Zα domain of the PKZ from Carassius auratus (caZαPKZ) 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 caZαPKZat 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 caZαPKZcan be used as molecular ruler to measure the degree of B-Z transition.
authors.affiliation: Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of Korea.
authors.forename: Ae-Ree
authors.initials: AR
authors.lastname: Lee
authors.affiliation: Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of Korea.
authors.forename: Yeo-Jin
authors.initials: YJ
authors.lastname: Seo
authors.affiliation: Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of Korea.
authors.forename: Seo-Ree
authors.initials: SR
authors.lastname: Choi
authors.affiliation: Division of Magnetic Resonance, KBSI, Chungbuk 28119, Republic of Korea.
authors.forename: Kyoung-Seok
authors.initials: KS
authors.lastname: Ryu
authors.affiliation: Division of Magnetic Resonance, KBSI, Chungbuk 28119, Republic of Korea.
authors.forename: Hae-Kap
authors.initials: HK
authors.lastname: Cheong
authors.affiliation: Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of Korea.
authors.forename: Shim Sung
authors.initials: SS
authors.lastname: Lee
authors.affiliation: Institute of Advanced Energy, Kyoto University, Kyoto 611-0011, Japan.
authors.forename: Masato
authors.initials: M
authors.lastname: Katahira
authors.affiliation: Department of Chemistry, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea. Electronic address: cjpark@gist.ac.kr.
authors.forename: Chin-Ju
authors.initials: CJ
authors.lastname: Park
authors.affiliation: Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of Korea; Division of Magnetic Resonance, KBSI, Chungbuk 28119, Republic of Korea. Electronic address: joonhwa@gnu.ac.kr.
authors.forename: Joon-Hwa
authors.initials: JH
authors.lastname: Lee
mesh_terms: D001665:Binding Sites; D059371:DNA, B-Form / Q000737:chemistry* / Q000648:ultrastructure; D043542:DNA, Z-Form / Q000737:chemistry* / Q000648:ultrastructure; D004789:Enzyme Activation; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011485:Protein Binding; D011494:Protein Kinases / Q000737:chemistry* / Q000648:ultrastructure*; D012965:Sodium Chloride / Q000737:chemistry*; D029961:Zebrafish Proteins / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D059371:DNA, B-Form; D043542:DNA, Z-Form; D029961:Zebrafish Proteins; D012965:Sodium Chloride; C583881:PKZ protein, zebrafish; D011494:Protein Kinases
keywords: DNA-protein interaction; NMR; Salt effect; Z-DNA; Z-DNA binding protein