6533b872fe1ef96bd12d3abe
RESEARCH PRODUCT
Molecular cloning and evolution of lobster hemocyanin.
Thorsten BurmesterKristina Kuschesubject
Protein subunitmedicine.medical_treatmentMolecular Sequence DataBiophysicsMolecular cloningBiochemistryEvolution MolecularComplementary DNAmedicineAnimalsTissue DistributionAmino Acid SequenceRNA MessengerCloning MolecularMolecular clockMolecular BiologyPhylogenyHomarusMolecular massbiologySequence Homology Amino AcidHemocyaninCell BiologyAmerican lobsterbiology.organism_classificationMolecular biologyNephropidaeProtein SubunitsHemocyaninsdescription
In the American lobster, Homarus americanus, oxygen is transported by a hemocyanin that is composed 2 x 6 subunits. N-terminal sequencing show the presence of three distinct subunit types (alpha, beta and gamma). We cloned the cDNA of one of these subunits that belong to the alpha-type. It encodes a hemocyanin subunit of 654 amino acids with a molecular mass of 84.8 kDa, which is synthesized in the hepatopancreas. Phylogenetic analyses of the crustacean hemocyanin sequences show two well-separated clades, which correspond to the alpha and gamma-type subunits. Sequences of beta-type subunits are still unknown. The gamma-sequences have evolved about 15% faster than the alpha-subunits, consistent with the proposed conservative function of the latter. Under the assumption of a molecular clock we calculated that alpha- and gamma-subunits split about 214 +/- 14 million years ago, suggesting their divergence only in the decapod Crustacea.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-04-01 | Biochemical and biophysical research communications |