Research Article

Molecular cloning and cDNA characterization of Camelus dromedarius putative cytochrome P450s 1A, 2C, and 3A

Published: March 17, 2014
Genet. Mol. Res. 13 (2) : 2886-2905 DOI: 10.4238/2014.March.17.1

Abstract

The domesticated one-humped Arabian camel, Camelus dromedarius, is one of the most important animals in the Arabian Peninsula. Most of its life, this animal is exposed to both intrinsic and extrinsic genotoxic factors that are known to cause gross metabolic alterations in many organisms. This study determined the full length coding sequence of 3 cytochrome P450s cDNAs; namely, CYP450 1A1, CYP450 2C and CYP450 3A using reverse transcription polymerase chain reaction. The C. dromedarius CYP450s 1A1, 2C, and 3A have open reading frames of 1563, 1473, and 1566 bp and cDNAs that encode proteins of 520, 490, and 521 amino acid residues, respectively. The molecular weights calculated for CYP1A1, 2C, and 3A were found to be 58.651, 56.03, and 58.594 kDa, while the predicted calculated isoelectric points using a computer algorithm were 7.315, 6.579, and 9.46. The deduced amino acid sequences of these CYPs showed the membrane anchored signal peptide, the conserved proline-rich amino terminus and the characteristic heme-binding signature localized near the carboxy terminus of the protein.

The domesticated one-humped Arabian camel, Camelus dromedarius, is one of the most important animals in the Arabian Peninsula. Most of its life, this animal is exposed to both intrinsic and extrinsic genotoxic factors that are known to cause gross metabolic alterations in many organisms. This study determined the full length coding sequence of 3 cytochrome P450s cDNAs; namely, CYP450 1A1, CYP450 2C and CYP450 3A using reverse transcription polymerase chain reaction. The C. dromedarius CYP450s 1A1, 2C, and 3A have open reading frames of 1563, 1473, and 1566 bp and cDNAs that encode proteins of 520, 490, and 521 amino acid residues, respectively. The molecular weights calculated for CYP1A1, 2C, and 3A were found to be 58.651, 56.03, and 58.594 kDa, while the predicted calculated isoelectric points using a computer algorithm were 7.315, 6.579, and 9.46. The deduced amino acid sequences of these CYPs showed the membrane anchored signal peptide, the conserved proline-rich amino terminus and the characteristic heme-binding signature localized near the carboxy terminus of the protein.