TY - JOUR
T1 - Molecular cloning and evolution of lobster hemocyanin
AU - Kusche, Kristina
AU - Burmester, Thorsten
N1 - Funding Information:
We thank J. Markl for the excellent working facilities and continuous support, H. Storz and W. Gebauer for their help with protein purification, and H. Heid for N-terminal sequence analysis. This work is supported by a grant of the Deutsche Forschungsgemein-schaft (Bu956/3). The nucleotide sequence reported in this paper has been submitted to the EMBL/GenBank Nucleotide Sequence Databases under the Accession No. AJ272095.
PY - 2001
Y1 - 2001
N2 - In the American lobster, Homarus americanus, oxygen is transported by a hemocyanin that is composed 2 × 6 subunits. N-terminal sequencing show the presence of three distinct subunit types (α, β and γ). We cloned the cDNA of one of these subunits that belong to the α-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 α and γ-type subunits. Sequences of β-type subunits are still unknown. The γ-sequences have evolved about 15% faster than the α-subunits, consistent with the proposed conservative function of the latter. Under the assumption of a molecular clock we calculated that α- and γ-subunits split about 214 ± 14 million years ago, suggesting their divergence only in the decapod Crustacea.
AB - In the American lobster, Homarus americanus, oxygen is transported by a hemocyanin that is composed 2 × 6 subunits. N-terminal sequencing show the presence of three distinct subunit types (α, β and γ). We cloned the cDNA of one of these subunits that belong to the α-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 α and γ-type subunits. Sequences of β-type subunits are still unknown. The γ-sequences have evolved about 15% faster than the α-subunits, consistent with the proposed conservative function of the latter. Under the assumption of a molecular clock we calculated that α- and γ-subunits split about 214 ± 14 million years ago, suggesting their divergence only in the decapod Crustacea.
UR - http://www.scopus.com/inward/record.url?scp=0034815460&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2001.4660
DO - 10.1006/bbrc.2001.4660
M3 - Journal articles
C2 - 11352633
AN - SCOPUS:0034815460
SN - 0006-291X
VL - 282
SP - 887
EP - 892
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -