The hemocyanin from a living fossil, the cephalopod Nautilus pompilius: protein structure, gene organization, and evolution

Journal of Molecular Evolution
Sandra BergmannJ Markl

Abstract

By electron microscopic and immunobiochemical analyses we have confirmed earlier evidence that Nautilus pompilius hemocyanin (NpH) is a ring-like decamer (M(r) = approximately 3.5 million), assembled from 10 identical copies of an approximately 350-kDa polypeptide. This subunit in turn is substructured into seven sequential covalently linked functional units of approximately 50 kDa each (FUs a-g). We have cloned and sequenced the cDNA encoding the complete polypeptide; it comprises 9198 bp and is subdivided into a 5' UTR of 58 bp, a 3' UTR of 365 bp, and an open reading frame for a signal peptide of 21 amino acids plus a polypeptide of 2903 amino acids (M(r) = 335,881). According to sequence alignments, the seven FUs of Nautilus hemocyanin directly correspond to the seven FU types of the previously sequenced hemocyanin "OdH" from the cephalopod Octopus dofleini. Thirteen potential N-glycosylation sites are distributed among the seven Nautilus hemocyanin FUs; the structural consequences of putatively attached glycans are discussed on the basis of the published X-ray structure for an Octopus dofleini and a Rapana thomasiana FU. Moreover, the complete gene structure of Nautilus hemocyanin was analyzed; it resembles that of Octopus...Continue Reading

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Citations

May 4, 2007·Journal of Molecular Evolution·Sandra BergmannBernhard Lieb
Mar 24, 2004·Micron : the International Research and Review Journal for Microscopy·Bernhard Lieb, Jürgen Markl
May 15, 2010·Frontiers in Zoology·Bernhard LiebJürgen Markl
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Jan 12, 2020·Communications Biology·Christian KlugRené Hoffmann
Mar 6, 2021·BMC Ecology and Evolution·Gabriela Giannina SchäferBernhard Lieb
May 12, 2021·Nature Ecology & Evolution·Yang ZhangZiniu Yu
Nov 11, 2021·Journal of Molecular Evolution·Gabriela Giannina SchäferBernhard Lieb

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