CDNA cloning and sequencing of Octopus dofleini hemocyanin Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/w3763871s

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  • Hemocyanins are oxygen transport molecules found only in molluscs and arthropods. They are very large molecules with molecular weights in the range of several million Daltons. They are multisubunit aggregates and their oxygen binding site contains a binuclear copper center. Molluscan and arthropodan hemocyanins are fundamentally different in structure and it has been of interest for a long time whether both proteins are products of divergent or convergent evolution. It was clear that sequence data were needed from both proteins in order to resolve this question. Our laboratory is investigating the structure and function of Octopus dofleini hemocyanin. It consists of ten polypeptide chains of 350,000 Da each. Each subunit is composed of seven domains. In order to sequence hemocyanin recombinant DNA methods were chosen, because conventional protein sequencing methods seemed not feasible. Complementary DNA clones coding for three domains at the C-terminal end of hemocyanin were isolated and sequenced. Comparison of these sequences with those of arthropodan hemocyanins showed no similarity, except for a small region corresponding to the "Copper B" site. Molluscan hemocyanins are more closely related to tyrosinases than they are to arthropodan hemocyanins. Sequence comparisons with domains of other recently published molluscan hemocyanins showed that molluscan hemocyanins already existed in the precambrian before the molluscan orders diverged from each other in the early cambrium. Sequence comparisons of molluscan hemocyanins with tyrosinases allowed us to identify potential ligands for the "Copper A" site, whose structure, unlike in arthropodan hemocyanins, is different from the "Copper B" site.
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