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The Analyses of Cetacean Virus-Responsive Genes Reveal Evolutionary Marks in Mucosal Immunity-Associated Genes
Viruses are the most common and abundant organisms in the marine environment. To better understand how cetaceans have adapted to this virus-rich environment, we compared cetacean virus-responsive genes to those from terrestrial mammals. We identified virus-responsive gene sequences in seven species of cetaceans, which we compared with orthologous sequences in seven terrestrial mammals. As a result of evolution analysis using the branch model and the branch-site model, 21 genes were selected using at least one model. IFN-epsilon, an antiviral cytokine expressed at mucous membranes, and its receptor IFNAR1 contain cetacean-specific amino acid substitutions that might change the interaction between the two proteins and lead to regulation of the immune system against viruses. Cetacean-specific amino acid substitutions in IL-6, IL-27, and the signal transducer and activator of transcription (STAT)1 are also predicted to alter the mucosal immune response of cetaceans. Since mucosal membranes are the first line of defense against the external environment and are involved in immune tolerance, our analysis of cetacean virus-responsive genes suggests that genes with cetacean-specific mutations in mucosal immunity-related genes play an important role in the protection and/or regulation of immune responses against viruses
Soil liquefaction potential assessment using ambient noise: A case study in Pohang, Korea
An M ( W ) 5.5 earthquake occurred in Pohang, Korea, on 15 November 2017 and caused large damage. In and around the epicentral area the earthquake also remained numerous sand boils, which is a surface representation of soil liquefaction at shallow depth during the earthquake. Soil liquefaction is one of the most dangerous consequences of an earthquake. Here we show that the spatial distribution of the ground vulnerability index (K ( g )), which we estimate via ambient noise analysis, correlates very well with the distribution of sand boils. Our K ( g ) model based on the dense microtremor surveys at differing geological conditions and urbanizations indicates that only 28.4% of the study area is vulnerable to ground shaking (K ( g ) > 20), with 91.1% of the observed sand boils occurring in these vulnerable areas. We also observed that K ( g ) values estimated in the study correlate well with both V ( S30 ) values and geologic units in the study area. This case report confirmed that the K ( g ) can be an affordable supplement to traditional, but expensive and time-consuming, geotechnical/geophysical techniques for the initial screening and regional evaluations. Such a K ( g ) map can assist stakeholders in earthquake-prone regions in identifying areas more susceptible to liquefaction and bring a recommendation to consider seismic hazard mitigation
Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1
Aminoacyl-tRNA synthetases possess unique domains. In this study the structure of the vertebrate IARS1 and EARS1 complex reveals that vertebrate IARS1 protects the DNA repair factor BRCA1 from proteolytic degradation via its UBX-fold domain. Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function