Comparison of Haliotis rubra hemocyanin isoforms 1 and 2

Jiadai Wu, Anthony L. Cunningham, Fariba Dehghani, Russell J. Diefenbach*

*Corresponding author for this work

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

We have obtained for the first time the complete cDNA sequences encoding the two known hemocyanin isoforms from the mollusc Haliotis rubra. Based on the predicted amino acid sequence each isoform has an almost identical estimated molecular mass of ~ 390 kDa. The isoforms share an amino acid sequence similarity of 66% and consist of eight functional units (FUs a-h) separated by variable linker regions. As observed in other molluscan hemocyanins, FU-h has a C-terminal extension of ~ 100 amino acids. The presence of a conserved di-copper binding domain in each FU, which contributes to hemocyanin's role as an oxygen transporter, was also confirmed. The most closely related sequences to H. rubra were those of the hemocyanin isoforms from Haliotis tuberculata with a homology of > 90%. Like the hemocyanin isoforms from H. tuberculata, the H. rubra versions contain several predicted N-linked glycosylation sites. The predicted N-linked glycosylation pattern of H. rubra hemocyanin isoforms is highly similar but not identical to H. tuberculata hemocyanin isoforms. Such differences may translate to variations in structural organisation of these oligomeric proteins or in other known functions of hemocyanin such as innate immunity or antiviral activity. Knowledge of the complete cDNA sequences of H. rubra hemocyanin isoforms will allow mapping of minimal domain(s) required for these functions.

Original languageEnglish
Pages (from-to)123-130
Number of pages8
JournalGene Reports
Volume4
DOIs
Publication statusPublished - 1 Sep 2016
Externally publishedYes

Keywords

  • oxygen binding
  • oxygen transport
  • protein structure
  • structural biology
  • structural model
  • tyrosinase

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