The changing form of Antarctic biodiversity

Antarctic biodiversity is much more extensive, ecologically diverse and biogeographically structured than previously thought. Understanding of how this diversity is distributed in marine and terrestrial systems, the mechanisms underlying its spatial variation, and the significance of the microbiota is growing rapidly. Broadly recognizable drivers of diversity variation include energy availability and historical refugia. The impacts of local human activities and global environmental change nonetheless pose challenges to the current and future understanding of Antarctic biodiversity. Life in the Antarctic and the Southern Ocean is surprisingly rich, and as much at risk from environmental change as it is elsewher

A Ca2+-dependent bacterial antifreeze protein domain has a novel b-helical ice-binding fold

AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large (>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned, expressed and characterized a 322-amino-acid region of the protein where the antifreeze activity is localized that shows similarity to the RTX (repeats-in-toxin) family of proteins. The recombinant protein requires Ca2+ for structure and activity, and it is capable of depressing the freezing point of a solution in excess of 2°C at a concentration of 0.5 mg/ml, therefore classifying it as a hyperactive AFP. We have developed a homology-guided model of the antifreeze region based partly on the Ca2+-bound b-roll from alkaline protease. The model has identified both a novel b-helical fold and an ice-binding site. The interior of the b-helix contains a single row of bound Ca2+ ions down one side of the structure and a hydrophobic core down the opposite side. The ice-binding surface consists of parallel repetitive arrays of threonine and aspartic acid/asparagine residues located down the Ca2+-bound side of the structure. The model was tested and validated by site-directed mutagenesis. It explains the Ca2+-dependency of the region, as well its hyperactive antifreeze activity. This is the first bacterial AFP to be structurally characterized and is one of only five hyperactive AFPs identified to date

A Ca2+ dependent bacterial antifreeze protein domain has a novel beta-helical ice-binding fold

AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large (>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned, expressed and characterized a 322-amino-acid region of the protein where the antifreeze activity is localized that shows similarity to the RTX (repeats-in-toxin) family of proteins. The recombinant protein requires Ca2+ for structure and activity, and it is capable of depressing the freezing point of a solution in excess of 2°C at a concentration of 0.5 mg/ml, therefore classifying it as a hyperactive AFP. We have developed a homology-guided model of the antifreeze region based partly on the Ca2+-bound β- roll from alkaline protease. The model has identified both a novel β-helical fold and an ice-binding site. The interior of the !-helix contains a single row of bound Ca2+ ions down one side of the structure and a hydrophobic core down the opposite side. The icebinding surface consists of parallel repetitive arrays of threonine and aspartic acid/asparagine residues located down the Ca2+- bound side of the structure. The model was tested and validated by site-directed mutagenesis. It explains the Ca2+-dependency of the region, as well its hyperactive antifreeze activity. This is the first bacterial AFP to be structurally characterized and is one of only five hyperactive AFPs identified to date

A Ca²⁺ dependent bacterial antifreeze protein domain has a novel beta-helical ice-binding fold

AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large (>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned, expressed and characterized a 322-amino-acid region of the protein where the antifreeze activity is localized that shows similarity to the RTX (repeats-in-toxin) family of proteins. The recombinant protein requires Ca2+ for structure and activity, and it is capable of depressing the freezing point of a solution in excess of 2°C at a concentration of 0.5 mg/ml, therefore classifying it as a hyperactive AFP. We have developed a homology-guided model of the antifreeze region based partly on the Ca2+-bound β- roll from alkaline protease. The model has identified both a novel β-helical fold and an ice-binding site. The interior of the !-helix contains a single row of bound Ca2+ ions down one side of the structure and a hydrophobic core down the opposite side. The icebinding surface consists of parallel repetitive arrays of threonine and aspartic acid/asparagine residues located down the Ca2+- bound side of the structure. The model was tested and validated by site-directed mutagenesis. It explains the Ca2+-dependency of the region, as well its hyperactive antifreeze activity. This is the first bacterial AFP to be structurally characterized and is one of only five hyperactive AFPs identified to date

Heterotrophic bacterial and viral dynamics in Arctic freshwaters: results from a field study and nutrient-temperature manipulation experiments

Heterotrophic bacterial and viral concentrations (range, 0.7 x 10(4) to 206.2 x 10(4) ml(-1) and 0.05 x 10(6) to 128.9 x 10(6) ml(-1), respectively) were determined in several Arctic freshwater environments, including lakes and glacial ecosystems (78.55 degrees N, 11.56 degrees E). Our bacteria and virus results mirrored trends seen in temperate lakes, with an average virus-to-bacteria ratio (VBR) of 13 (range, 7.3-25.2) and viral concentrations and DOC positively correlated with bacterial concentrations (R = 0.964, P < 0.01 and R = 0.813, P < 0.05, respectively). Lysogenic bacteria, determined by induction with Mitomycin C, were not detected in any of the investigated Arctic freshwater environments. Nutrient-addition experiments at in situ and at elevated temperatures were performed to elucidate the factors which influenced the bacterial growth and the virus-bacteria interactions in Arctic freshwaters. Our results suggest that multiple limiting factors interacted and constrained bacterial growth. Bacterial concentrations and doubling times increased at elevated temperatures and appeared to be co-stimulated by phosphorus and carbon. However, viral concentrations showed a lack of response to nutrient addition thus indicating an uncoupling between bacteria and viruses in the experiment