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Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.


ABSTRACT: Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune response and viral infection. Structural and biophysical studies show that ZBPs initially form an intermediate complex with B-DNA for B-Z conversion. However, a comprehensive understanding of the mechanism of Z-DNA binding and B-Z transition is still lacking, due to the absence of structural information on the intermediate complex. Here, we report the solution structure of the Z? domain of the ZBP-containing protein kinase from Carassius auratus(caZ?PKZ). We quantitatively determined the binding affinity of caZ?PKZ for both B-DNA and Z-DNA and characterized its B-Z transition activity, which is modulated by varying the salt concentration. Our results suggest that the intermediate complex formed by caZ?PKZ and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform.

SUBMITTER: Lee AR 

PROVIDER: S-EPMC4824103 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.

Lee Ae-Ree AR   Park Chin-Ju CJ   Cheong Hae-Kap HK   Ryu Kyoung-Seok KS   Park Jin-Wan JW   Kwon Mun-Young MY   Lee Janghyun J   Kim Kyeong Kyu KK   Choi Byong-Seok BS   Lee Joon-Hwa JH  

Nucleic acids research 20160120 6


Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune response and viral infection. Structural and biophysical studies show that ZBPs initially form an intermediate complex with B-DNA for B-Z conversion. However, a comprehensive understanding of the mechanism of Z-DNA binding and B-Z transition is still lacking, due to the absence of structural information on the intermediate complex. Here, we report the solution structure of the Zα domain of the ZBP-containing protein  ...[more]

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