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Fragilariopsis is a dominating psychrophilic diatom genus in polar sea ice. The two species Fragilariopsis cylindrus and Fragilariopsis curta are able to grow and divide below freezing temperature of sea water and above average sea water salinity. Here we show that antifreeze proteins (AFPs), involved in cold adaptation in several psychrophilic organisms, are widespread in the two polar species. The presence of AFP genes (afps) as a multigene family indicated the importance of this group of genes for the genus Fragilariopsis, possibly contributing to its success in sea ice. Protein phylogeny showed the potential mobility of afps, which appear to have crossed kingdom and domain borders, occurring in Bacteria, diatoms, crustaceans and fungi. Our results revealed a broad distribution of AFPs not only in polar organisms but also in taxa apparently not related to cold environments, suggesting that these proteins may be multifunctional. The relevance of AFPs to Fragilariopsis was also shown by gene expression analysis. Under stress conditions typical for sea ice, with subzero temperatures and high salinities, F. cylindrus and F. curta strongly expressed selected afps. An E/G point mutation in the Fragilariopsis AFPs may play a role in gene expression activity and protein function.

ABSTRACT:The low temperatures of polar regions and high altitude environments, especially icy habitats, present challenges for many microorganisms. Their ability to live under subfreezing conditions implies the production of compounds conferring cryotolerance. Colwellia psychrerythraea 34H, a -proteobacterium isolated from subzero Arctic marine sediments, provides a model for the study of life in cold environments. We report here the identification and detailed molecular primary and secondary structures of capsular polysaccharide from C. psychrerythraea 34H cells. The polymer was isolated in the water layer when cells were extracted by phenol/water and characterized by one-and two-dimensional NMR spectroscopy together with chemical analysis. Molecular mechanic and dynamic calculations were also performed. The polysaccharide consists of a tetrasaccharidic repeating unit containing two amino sugars and two uronic acids bearing threonine as substituent. The structural features of this unique polysaccharide resemble those present in antifreeze proteins and glycoproteins. These results suggest a possible correlation between the capsule structure and the ability of C. psychrerythraea to colonize subfreezing marine environments.

Abstract. Impurities control a variety of physical properties of polar ice. Their impact can be observed at all scalesfrom the microstructure (e.g., grain size and orientation) to the ice sheet flow behavior (e.g., borehole tilting and closure). Most impurities in ice form micrometer-sized inclusions. It has been suggested that these µ inclusions control the grain size of polycrystalline ice by pinning of grain boundaries (Zener pinning), which should be reflected in their distribution with respect to the grain boundary network. We used an optical microscope to generate high-resolution large-scale maps (3 µm pix −1 , 8×2 cm 2 ) of the distribution of micro-inclusions in four polar ice samples: two from Antarctica (EDML, MIS 5.5) and two from Greenland (NEEM, Holocene). The in situ positions of more than 5000 µ inclusions have been determined. A Raman microscope was used to confirm the extrinsic nature of a sample proportion of the mapped inclusions. A superposition of the 2-D grain boundary network and µ-inclusion distributions shows no significant correlations between grain boundaries and µ inclusions. In particular, no signs of grain boundaries harvesting µ inclusions could be found and no evidence of µ inclusions inhibiting grain boundary migration by slow-mode pinning could be detected. Consequences for our understanding of the impurity effect on ice microstructure and rheology are discussed.

Ice‐binding proteins (IBPs) control the growth and shape of ice crystals to cope with subzero temperatures in psychrophilic and freeze‐tolerant organisms. Recently, numerous proteins containing the domain of unknown function (DUF) 3494 were found to bind ice crystals and, hence, are classified as IBPs. DUF3494 IBPs constitute today the most widespread of the known IBP families. They can be found in different organisms including bacteria, yeasts and microalgae, supporting the hypothesis of horizontal transfer of its gene. Although the 3D structure is always a discontinuous β‐solenoid with a triangular cross‐section and an adjacent alpha‐helix, DUF3494 IBPs present very diverse activities in terms of the magnitude of their thermal hysteresis and inhibition of ice recrystallization. The proteins are secreted into the environments around the host cells or are anchored on their cell membranes. This review covers several aspects of this new class of IBPs, which promise to leave their mark on several research fields including structural biology, protein biochemistry and cryobiology.