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Nucleic Acids Research, 1989, Vol. 17, No. 8 2907-2917
© 1989

MOLECULAR BIOLOGY

Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity

John S. Miles, Wendy Bickmore1, J.David Brook2, Aileen W. McLaren, Richard Meeham1,+ and C.Ronald Wolf*

Imperial Cancer Research Fund, Laboratory of Molecular Pharmacology, University Department of Biochemistry Hugh Robson Building, George Square, Edinburgh EH8 9XD, UK 1Research Council, Human Genetics Unit Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK 2Institute of Medical Genetics, University of Wales College of Medecine Heath Park, Cardiff CF4 4XN, UK

*To whom correspondence should be addressed

Received February 16, 1989. Accepted March 23, 1989.

We have isolated from human liver libraries two cytochrome P450 cDNA clones ({lambda}MP14 and {lambda}XMP3) which are highly similar (83% over the coding region) to mouse testosterone 15{alpha} hydroxylase and are therefore part of the cytochrome P450IIA gene subfamily. The P450IIA (CYP2A) gene subfamily was found to be closely linked to the P450IIB (CYP2B) subfamily and their chromosomal location could not be distinguished using somatic cell hybrids containing fragments of chromosome 19 between 19q12 and 19q13.2. Pulsed field gel electrophoresis indicates that both gene subfamilies are contained within 350-kb genomic DNA fragments, but were separated using various restriction enzymes. Northern blot analysis identified three P450IIA mRNAs each showing a wide inter-individual variation in their levels in the liver. High levels of P450IIA transcript were associated with high levels of P450IIB transcript suggesting that common factors may influence the expression of genes within these subfamilies. Genetic analysis has suggested previously that a member of the P450IIB subfamily is responsible for coumarin hydroxylase activity in the mouse. We discuss the possibility, based on our findings of tight linkage of the human P450IIA and IIB subfamilies, that a member of the IIA subfamily is a better candidate for this enzyme activity.

+Present address: Institute of Molecular Pathology, Dr Bohr Gasse 7, A1030 Wein, Austria


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