2rvc

Publication Abstract from PubMed

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 Zalpha domain of the ZBP-containing protein kinase from Carassius auratus (caZalphaPKZ). We quantitatively determined the binding affinity of caZalphaPKZ 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 caZalphaPKZ and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform.

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 AR, Park CJ, Cheong HK, Ryu KS, Park JW, Kwon MY, Lee J, Kim KK, Choi BS, Lee JH Nucleic Acids Res. 2016 Jan 20. pii: gkw025. PMID:26792893^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.