Adaptation is driven by natural selection; however, many adaptations are caused by weak selection acting over large timescales, complicating its study. Therefore, it is rarely possible to study selection comprehensively in natural environments. The threespine stickleback (Gasterosteus aculeatus) is a well-studied model organism with a short generation time, small genome size, and many genetic and genomic tools available. Within this originally marine species, populations have recurrently adapted to freshwater all over its range. This evolution involved extensive parallelism: pre-existing alleles that adapt sticklebacks to freshwater habitats, but are also present at low frequencies in marine populations, have been recruited repeatedly. While a number of genomic regions responsible for this adaptation have been identified, the details of selection remain poorly understood. Using whole-genome resequencing, we compare pooled genomic samples from marine and freshwater populations of the White Sea basin, and identify 19 short genomic regions that are highly divergent between them, including three known inversions. 17 of these regions overlap protein-coding genes, including a number of genes with predicted functions that are relevant for adaptation to the freshwater environment. We then analyze four additional independently derived young freshwater populations of known ages, two natural and two artificially established, and use the observed shifts of allelic frequencies to estimate the strength of positive selection. Adaptation turns out to be quite rapid, indicating strong selection acting simultaneously at multiple regions of the genome, with selection coefficients of up to 0.27. High divergence between marine and freshwater genotypes, lack of reduction in polymorphism in regions responsible for adaptation, and high frequencies of freshwater alleles observed even in young freshwater populations are all consistent with rapid assembly of G. aculeatus freshwater genotypes from pre-existing genomic regions of adaptive variation, with strong selection that favors this assembly acting simultaneously at multiple loci.

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The taxonomy of common northern nudibranch molluscs of the genus Dendronotus in the vast cold regions of Eurasia remains largely unknown. Abundant material collected in many localities from the Barents Sea, via the Arctic region, to the north-west Pacific was analysed for the first time. An integrated approach combining morphological and ontogenetic data with molecular four-gene (COI, 16S, H3, and 28S) analysis reveals seven species, including three previously undescribed. Dendronotus frondosus (Ascanius, 1774) and Dendronotus dalli Bergh, 1879 were commonly considered as amphiboreal species; however, according to this study they are restricted to the North Atlantic and the North Pacific, respectively. In the north-west Pacific two new species were discovered, Dendronotus kamchaticus sp. nov. and Dendronotus kalikal sp. nov., that are externally similar to D. frondosus, but that show significant distance according to molecular analysis and are considerably different in radular morphology. In the North Atlantic a new species Dendronotus niveus sp. nov., sibling to North Pacific D. dalli, is revealed. The separate status of North Atlantic Dendronotus lacteus (Thompson, 1840) is confirmed, including considerable range extension. The essential similarity of early ontogenetic stages of radular development common for species with disparate adult radular morphology (such as D. frondosus and D. dalli) is shown, and its importance for taxonomy is discussed.

Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins--spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in Pichia pastoris and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 microm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel beta-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery.