期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 52, 页码 30713-30725出版社
ELSEVIER
DOI: 10.1074/jbc.M115.679407
关键词
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资金
- Fundacao para a Ciencia ea Tecnologia [PTDC/BIA-PRO/112962/2009, IF/00641/2013]
- European Community [283570]
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-PRO/112962/2009] Funding Source: FCT
In vertebrate species, the innate immune system down-regulates protein translation in response to viral infection through the action of the double-stranded RNA (dsRNA)-activated protein kinase (PKR). In some teleost species another protein kinase, Z-DNA-dependent protein kinase (PKZ), plays a similar role but instead of dsRNA binding domains, PKZ has Z alpha domains. These domains recognize the left-handed conformer of dsDNA and dsRNA known as Z-DNA/Z-RNA. Cyprinid herpesvirus 3 infects common and koi carp, which have PKZ, and encodes the ORF112 protein that itself bears a Z alpha domain, a putative competitive inhibitor of PKZ. Here we present the crystal structure of ORF112-Z alpha in complex with an 18-bpCpGDNA repeat, at 1.5 angstrom. We demonstrate that the bound DNA is in the left-handed conformation and identify key interactions for the specificity of ORF112. Localization of ORF112 protein in stress granules induced in Cyprinid herpesvirus 3-infected fish cells suggests a functional behavior similar to that of Z alpha domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI.
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