Isolation of a full-length cDNA encoding mouse aro...[Arch Biochem Biophys. 1991]

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1: Arch Biochem Biophys. 1991 Mar;285(2):231-7.Links

Isolation of a full-length cDNA encoding mouse aromatase P450.

Terashima M, Toda K, Kawamoto T, Kuribayashi I, Ogawa Y, Maeda T, Shizuta Y.

Department of Medical Chemistry, Kochi Medical School, Japan.

A full-length cDNA clone for aromatase P450 has been isolated from a pregnant mouse ovarian cDNA library. The insert of this clone (2394 bp) contains a 1509-bp open reading frame encoding 503 amino acid residues together with a 46-bp 5'-untranslated stretch and an 839-bp 3'-untranslated region to which a poly(A) tract is attached. Northern blot analysis of ovarian RNA from pregnant mice reveals a major mRNA band of 2.5 kb with a minor band of 2.1 kb. Comparison of mouse aromatase P450 with that of rat, human, and chicken shows 91, 81, and 69% identity in the nucleotide sequence and 92, 79, and 69% identity in the deduced amino acid sequence, respectively. The membrane-spanning domain of mouse aromatase P450 is estimated to be an extremely hydrophobic segment located within the N-terminal region of the molecule. Furthermore, a highly conserved heme-binding domain is noticed.

PMID: 1897929 [PubMed - indexed for MEDLINE]

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Cited by 5 PubMed Central articles

The planetary biology of cytochrome P450 aromatases.
Gaucher EA, Graddy LG, Li T, Simmen RC, Simmen FA, Schreiber DR, Liberles DA, Janis CM, Benner SA. BMC Biol. 2004 Aug 17; 2:19. Epub 2004 Aug 17.

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Fisher CR, Graves KH, Parlow AF, Simpson ER. Proc Natl Acad Sci U S A. 1998 Jun 9; 95(12):6965-70.

[Proc Natl Acad Sci U S A. 1998]
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