Fine-scale estimations of bioclimatic change in the Valencia region, Spain

Recent advances in statistical downscaling have allowed the reconstruction of temperatures for the complete 1948–2011 period in a spatial resolution of 90 m and without gaps for the Valencian Community (Spain) and bordering areas. It presently enables analyses in this region, which allows the determination of recent temperature changes at subregional and local scales. The present work focuses on obtaining the thermicity index according to Rivas-Martínez, a well-known indicator of different thermotypes associated with bioclimatic horizons. The change in this index, which has happened in the region between 1948 and 2011, was calculated by generating fine-scale maps of the potential extension of different thermotypes. The results show a greater regression for the thermotypes in a finicolous position, e.g. Orotemperate, Supratemperate and Supramediterranean horizons, which herein indicate greater potential vulnerability in climate change. In the absence of, and given the need for, such fine-scale information, this work should be useful for specialized researchers to spatially limit the potentially most vulnerable biotopes to climate change.

The Structure of theCyprinid herpesvirus 3ORF112-Zα·Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Response

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 Zα 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 Zα domain, a putative competitive inhibitor of PKZ. Here we present the crystal structure of ORF112-Zα in complex with an 18-bp CpG DNA repeat, at 1.5 Å. 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 Zα domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI.