Cloning, sequencing, and characterization of CYP1A1 cDNA from leaping mullet (Liza saliens) liver and implications for the potential functions of its conserved amino acids

Date

2001-01-01

Author

Sen, A
Hu, CH
Urbach, E
Wang-Buhler, JL
Yang, YH
Arinc, E
Buhler, DR

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A 2,037 bp CYP1A1 cDNA (GenBank AF072899) was cloned through screening of a lambda ZipLox cDNA library constructed from the liver of a leaping mullet (Liza saliens) fish captured from Izmir Bay on the Aegean coast of Turkey using rainbow trout CYP1A1 cDNA as a probe. This clone has a 130 bp 5'-flanking region, a 1,563 bp open reading frame (ORF) encoding a 521-amino acid protein (58,972 Da), and a 344 bp 3'-untranslated region without a poly (A) tail. Alignment of the deduced amino acids of CYP1A1 cDNAs showed 58% and 69-96% identities with human and 12 other fish species, respectively. Southern blot analysis suggested that this CYP1A1 cDNA was from a single-copy gene. Based on the comparison with CYP1A1 genes reported for fish and mammals, the leaping mullet CYP1A1 gene is probably split into 7 exons. The intron insertion sites were predicted. Alignment of the CYP1A1 cDNA encoded amino acids from 13 fish and 7 mammalian species disclosed differences in highly conserved amino acids between aquatic and land vertebrates. The possible associated secondary structure; conserved motifs and substrate-binding sites were discussed. The phylogenetic relationships of CYP1A1s among 13 fish species were analyzed by a distance method. (C) 2001 John Wiley & Sons, Inc. J Biochem. Mol Toxicol 15:243-255, 2001.

Subject Keywords

Toxicology, Molecular Medicine, Biochemistry, Health, Toxicology and Mutagenesis, Molecular Biology, General Medicine

URI

https://hdl.handle.net/11511/68393

Journal

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY

DOI

https://doi.org/10.1002/jbt.10005

Collections

Department of Biology, Article

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Citation Formats

A. Sen et al., “Cloning, sequencing, and characterization of CYP1A1 cDNA from leaping mullet (Liza saliens) liver and implications for the potential functions of its conserved amino acids,” JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, pp. 243–255, 2001, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/68393.