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Antarctic Toothfish are a circumpolar species which are targeted in multiple fisheries around Antarctica covering nine statistical areas within the Convention for the Conservation of Antarctic Marine Living Resources. Despite this, it is still unclear whether the species forms a single stock across its circumpolar distribution, shows a pattern of isolation by distance, or exhibits discrete stock structure between different regions. Recent genetics studies of Antarctic toothfish have shown connectivity between two areas (Ross Sea and Antarctic Peninsula), but earlier studies with smaller number of markers produced inconsistent results with regards to genetic connectivity between other geographic locations. Here we present a range-wide population genetic study of Antarctic toothfish using > 11,000 nuclear single nucleotide polymorphisms from 715 fish collected. Our results indicate that genetic diversity of the Antarctic toothfish is very low, with only 0.1% of genetic variability associated with geographic location. Multiple clustering methods, both supervised and unsupervised, indicated no distinct breeding populations. These results are consistent with current theories of egg and larval dispersal by the predominant Antarctic currents. [ABSTRACT FROM AUTHOR]

The induction of highly conserved heat shock protein 70 (HSP70) is often related to a cellular response due to harmful stress or adverse life conditions. In this study, we determined the expression of Hsp70 genes in the Antarctic yeast, Glaciozyma antarctica, under different several thermal treatments for several exposure periods. The main aims of the present study were (1) to determine if stress-induced Hsp70 could be used to monitor the exposure of the yeast species G. antarctica to various types of thermal stress; (2) to analyze the structures of the G. antarctica HSP70 proteins using comparative modeling; and (3) to evaluate the relationship between the function and structure of HSP70 in G. antarctica. In this study, we managed to amplify and clone 2 Hsp70 genes from G. antarctica named GaHsp70-1 and GaHsp70-2. The cells of G. antarctica expressed significantly inducible Hsp70 genes after the heat and cold shock treatments. Interestingly, GaHsp70-1 showed 2–6-fold higher expression than GaHsp70-2 after the heat and cold exposure. ATP hydrolysis analysis on both G. antarctica HSP70s proved that these psychrophilic chaperones can perform activities in a wide range of temperatures, such as at 37, 25, 15, and 4 °C. The 3D structures of both HSP70s revealed several interesting findings, such as the substitution of a β-sheet to loop in the N-terminal ATPase binding domain and some modest residue substitutions, which gave the proteins the flexibility to function at low temperatures and retain their functional activity at ambient temperatures. In conclusion, both analyzed HSP70s played important roles in the physiological adaptation of G. antarctica. [ABSTRACT FROM AUTHOR]