688 resultados para 327.94
Resumo:
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.
Resumo:
The Holocene development of a treed palsa bog and a peat plateau bog, located near the railroad to Churchill in the Hudson Bay Lowlands of northeastern Manitoba, was traced using peat macrofossil and radiocarbon analyses. Both sites first developed as wet rich fens through paludification of forested uplands around 6800 cal. yr BP. Results show a 20th-century age for the palsa formation and repeated periods of permafrost aggradation and collapse at the peat plateau site during the late Holocene. This timing of permafrost dynamics corroborates well with that inferred from previous studies on other permafrost peatlands in the same region. The developmental history of the palsa and peat plateau bogs is similar to that of adjacent permafrost-free fens, except for the specific frost heave and collapse features associated with permafrost dynamics. Permafrost aggradation and degradation is ascribed to regional climatic, local autogenic and other factors. Particularly the very recent palsa development can be assessed in terms of climatic changes as inferred from meteorological data and surface hydrological changes related to construction of the railroad. The results indicate that cold years with limited snowfall as well as altered drainage patterns associated with infrastructure development may have contributed to the recent palsa formation.