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Cloning and sequencing of cDNAs of the β‐globin gene family in carp
Author(s) -
Yoshizaki G.,
Hirono I.,
Aoki T.,
Takashima F.
Publication year - 1997
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1997.tb01131.x
Subject(s) - biology , complementary dna , globin , microbiology and biotechnology , carp , peptide sequence , cdna library , gene , common carp , amino acid , cloning (programming) , sequence analysis , nucleic acid sequence , molecular cloning , primer (cosmetics) , rapid amplification of cdna ends , genetics , cyprinus , fishery , chemistry , organic chemistry , fish <actinopterygii> , computer science , programming language
A total blood cell cDNA library was constructed using a 3‐year‐old carp Cyprinus carpio . A β‐globin cDNA (CβG1) was identified from the library by the polymerase chain reaction using a β‐globin‐specific primer deduced from the carp β‐globin‐A amino acid sequence. Also, five additional types of β‐globin cDNAs (CβG2∼6) were isolated by colony hybridization using CβG1 as a probe. Sequence analysis revealed that these CβGs encoded 147 amino acids, and the deduced amino acid sequences showed high identity (89·1–95·2%) to previously reported carp β‐globin amino acid sequences. The nucleotide sequences of the CβGs were very similar (identity 96·0–99·6%) and the expression levels of CβG1∼6 were 28·6, 28·6, 21·4, 14·3, 3·6 and 3·6% of the total number of cloned CβGs, respectively. Although the complete amino acid sequence identities between the CβGs and the β‐globin of higher vertebrates were low, functionally important regions such as the α‐βcontact region and haem contact region were well conserved. These data showed that, as in higher vertebrates, the adult carp has a multiple β‐globin gene family (at least six members). However, transcripts encoding four types of peptides (CβG1 type, CβG2 and 3 type, CβG5 type, and CβG4 and 6 type) were expressed at relatively high levels, this being a unique character of the carp haemoglobin system.