Primary structure of chain I of the heterodimeric hemoglobin from the blood clam Barbatia virescens.

Abstract

The blood clam Barbatia virescens has a heterodimeric hemoglobin in erythrocytes. Interestingly, the congeneric clams B. reeveana and B. lima contain quite different hemoglobins: tetramer and polymeric hemoglobin consisting of unusual didomain chain. The complete amino acid sequence of chain I of B. virescens has been determined. The sequence was mainly determined from CNBr peptides and their subpeptides, and the alignment of the peptides was confirmed by sequencing of PCR-amplified cDNA for B. virescens chain I. The cDNA-derived amino acid sequence matched completely with the sequence proposed from protein sequencing. B. virescens chain I is composed of 156 amino acid residues, and the molecular mass was calculated to be 18,387 D, including a heme group. The sequence of B. virescens chain I showed 35-42% sequence identity with those of the related clam Anadara trapezia and the congeneric clam B. reeveana. An evolutionary tree for Anadara and Barbatia chains clearly indicates that all of the chains are evolved from one ancestral globin gene, and that the divergence of chains has occurred in each clam after the speciation. The evolutionary rate for clam hemoglobins was estimated to be about four times faster than that of vertebrate hemoglobin. We suggest that blood clam hemoglobin is a physiologically less important molecule when compared with vertebrate hemoglobins, and so it evolved rapidly and resulted in a remarkable diversity in quaternary and subunit structure within a relatively short period.