Diplopod hemocyanin sequence and the phylogenetic position of the Myriapoda

Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spiro...

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Bibliographic Details
Published in:Molecular biology and evolution 2001-08, Vol.18 (8), p.1566-1573
Main Authors: Kusche, K, Burmester, T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Arthropods - classification
Arthropods - genetics
Chilopoda
Cloning, Molecular
Diplopoda
DNA, Complementary - chemistry
DNA, Complementary - genetics
Evolution, Molecular
hemocyanin
Hemocyanins - chemistry
Hemocyanins - genetics
Molecular Sequence Data
Myriapoda
Pauropoda
Phylogeny
Sequence Alignment
Sequence Analysis, DNA
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Spirostreptidae
Spirostreptus
Symphyla
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Summary:Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two distinct subunits that are arranged in a 6 x 6 native molecule. The cloned hemocyanin subunit cDNA codes of for a polypeptide of 653 amino acids (75.5 kDa) that includes a signal peptide of 18 amino acids. The sequence closely resembles that of the chelicerate hemocyanins. Molecular phylogenetic analyses reject with high statistical confidence the integrity of the Tracheata (i.e., Myriapoda + Insecta) but give conflicting results on the position of the myriapod hemocyanin. While distance matrix and maximum-likelihood methods support a basal position of the Spirostreptus hemocyanin with respect to the other hemocyanins, parsimony analysis suggests a sister group relationship with the chelicerate hemocyanins. The latter topology is also supported by a unique shared deletion of an alpha-helix. A common ancestry of Myriapoda and Chelicerata should be seriously considered.
ISSN:0737-4038
1537-1719
DOI:10.1093/oxfordjournals.molbev.a003943