Thermomagnetic measurements on sediment cores GeoB1523-1, GeoB2910-1 and Geob4313-2

Low-temperature rock magnetic measurements have distinct diagnostic value. However, in most bulk marine sediments the concentration of ferrimagnetic and antiferromagnetic minerals is extremely low, so even sensitive instrumentation often responds to the paramagnetic contribution of the silicate matrix in the residual field of the magnetometer. Analysis of magnetic extracts is usually performed to solve the problems raised by low magnetic concentrations. Additionally magnetic extracts can be used for several other analyses, for example electron microscopy or X-ray diffraction. The magnetic extraction technique is generally sufficient for sediments dominated by magnetite. In this study however, we show that high-coercivity components are rather underrepresented in magnetic extracts of sediments with a more complex magnetic mineralogy. We test heavy liquid separation, using hydrophilic sodium polytungstenate solution Na6[H2W12O40], to demonstrate the efficiencies of both concentration techniques. Low-temperature cycling of zero-field-cooled, field-cooled and saturation isothermal remanent magnetization acquired at room temperature was performed on dry bulk sediments, magnetic extracts, and heavy liquid separates of clay-rich pelagic sediments originating from the Equatorial Atlantic. The results of the thermomagnetic measurements clarify that magnetic extraction favours components with high spontaneous magnetization, such as magnetite and titanomagnetite. The heavy liquid separation is unbiased with respect to high- and low-coercive minerals, thus it represents the entire magnetic assemblage.

DNA alignment and Bayesian trees of partial sequences of COI, COIII and the haemocyanin functional unit f-g of 28 octopod species

Background: Octopods have successfully colonised the world's oceans from the tropics to the poles. Yet, successful persistence in these habitats has required adaptations of their advanced physiological apparatus to compensate impaired oxygen supply. Their oxygen transporter haemocyanin plays a major role in cold tolerance and accordingly has undergone functional modifications to sustain oxygen release at sub-zero temperatures. However, it remains unknown how molecular properties evolved to explain the observed functional adaptations. We thus aimed to assess whether natural selection affected molecular and structural properties of haemocyanin that explains temperature adaptation in octopods. Results: Analysis of 239 partial sequences of the haemocyanin functional units (FU) f and g of 28 octopod species of polar, temperate, subtropical and tropical origin revealed natural selection was acting primarily on charge properties of surface residues. Polar octopods contained haemocyanins with higher net surface charge due to decreased glutamic acid content and higher numbers of basic amino acids. Within the analysed partial sequences, positive selection was present at site 2545, positioned between the active copper binding centre and the FU g surface. At this site, methionine was the dominant amino acid in polar octopods and leucine was dominant in tropical octopods. Sites directly involved in oxygen binding or quaternary interactions were highly conserved within the analysed sequence. Conclusions: This study has provided the first insight into molecular and structural mechanisms that have enabled octopods to sustain oxygen supply from polar to tropical conditions. Our findings imply modulation of oxygen binding via charge-charge interaction at the protein surface, which stabilize quaternary interactions among functional units to reduce detrimental effects of high pH on venous oxygen release. Of the observed partial haemocyanin sequence, residue 2545 formed a close link between the FU g surface and the active centre, suggesting a role as allosteric binding site. The prevalence of methionine at this site in polar octopods, implies regulation of oxygen affinity via increased sensitivity to allosteric metal binding. High sequence conservation of sites directly involved in oxygen binding indicates that functional modifications of octopod haemocyanin rather occur via more subtle mechanisms, as observed in this study.