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Molecular cloning of a family of xenobiotic-inducible drosophilid cytochrome P450s: Evidence for involvement in host-plant allelochemical resistance

  1. James C. Fogleman*
  1. *Department of Biological Sciences, 2101 East Wesley Avenue, University of Denver, Denver, CO 80208; and Section of Genetics and Development, 407 Biotechnology Building, Cornell University, Ithaca, NY 14853
  1. Edited by May R. Berenbaum, University of Illinois, Urbana, IL, and approved July 31, 1997

  1. Figure 1

    Analysis by Northern hybridization of the responsiveness of CYP28A1 (A), CYP28A2 (B), and CYP28A3 (C) to agria cactus triterpene glycosides (TTG), saguaro cactus alkaloids (Sag), senita cactus alkaloids (Sen), and phenobarbital (PB). Induction relative to untreated controls (−) was standardized to signal from a homologous rp49 probe. Images of the sequential cytochrome P450 and rp49 probings of the same blot have been superimposed. (Note: Interference from residual rRNA produces the “doublet-like” bands in the 3× Sag and PB lanes of C.)

  2. Figure 2

    Nucleotide and predicted amino acid sequences of CYP28A1 (A) and CYP28A2 (B). Amino acids are numbered on the left and nucleotides, on the right. Regions of conservation associated with helix I, helix K, and the heme-binding decapeptide are single-underlined. Putative polyadenylation signals are double-underlined.

  3. Figure 3

    Phylogram based on the single most parsimonious tree generated from the aligned full-length amino acid sequences of CYP28A1, CYP28A2, and representatives of the CYP3, CYP4, CYP6, and CYP9 families. The human mitochondrial CYP11A1 served as the outgroup. Branch lengths are indicated in terms of the predicted number of amino acid changes.

  4. Figure 4

    Alignment of the deduced amino acid sequences (helix L through translational stop) of CYP28A3 and CYP28A4 with CYP28A1 and CYP28A2. Identical amino acids are indicated by periods and differences, by the appropriate amino acid single-letter symbol.

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