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Molecular cloning of hemocyanin cDNA from Penaeus vannamei (Crustacea, Decapoda): structure, evolution and physiological aspects 1
Author(s) -
Sellos Daniel,
Lemoine Soazig,
Van Wormhoudt Alain
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00350-5
Subject(s) - hemocyanin , biology , hemolymph , hepatopancreas , complementary dna , untranslated region , open reading frame , microbiology and biotechnology , carcinus maenas , penaeus , crustacean , decapoda , messenger rna , shrimp , peptide sequence , biochemistry , genetics , gene , zoology , ecology , antigen
Hemocyanin is present as 2 subunits in the hemolymph of Penaeus vannamei . Isolated from a hepatopancreas cDNA library of this penaeid shrimp, the cDNA chain (2095 bp) corresponds to a full length hemocyanin messenger as determined by Northern hybridization, with a short 5′ untranslated region (17 bp), an open reading frame (1989 bp counting initiation and termination codons) coding for a signal peptide (13 residues) and a mature hemocyanin (648 amino acids), and a 3′ untranslated region (89 bp) followed by the polyadenylated track. It is the first time that the existence of a hydrophobic signal peptide is shown in arthropod hemocyanin. Two primary N‐terminal sequences are determined and a 3‐fold increase of mRNA content, measured in the hepatopancreas during the premoult stages, is reported. The low level of polymorphism shown by P. vannamei hemocyanin, along with its weak percentage identity with counterparts and its similarity with hemocyanin from Panulirus interruptus , suggests that this arthropod hemocyanin may be a primitive subunit that has evolved independently, following gene duplication.