Induction of CYP102 (cytochrome P450BM-3) in Bacillus megaterium by 17 beta-estradiol and 4-sec-butylphenol

Biochem Biophys Res Commun. 1998 Mar 27;244(3):868-72. doi: 10.1006/bbrc.1998.8170.

Abstract

CYP102 (Cytochrome P450BM-3) is induced in Bacillus megaterium by barbiturates, peroxisome proliferators, and nonsteroidal anti-inflammatory drugs. We now describe the induction of CYP102 in B. megaterium by 17 beta-estradiol and by 4-sec-butylphenol. These estrogens interact with the repressor protein Bm3R1, causing it to dissociate with the operator of the CYP102 gene and allowing transcription to occur. We have developed a stable transfection of a construct into B. megaterium of a truncated CYP102 gene coupled with the luciferase gene in a promoterless plasmid and have used this construct to test the induction of CYP102 by these estrogens. Estradiol demonstrated a dose-dependent induction of CYP102 which saturated at a 2-fold increase at 150 microM 4 hr post-addition. 4-sec-Butylphenol produced a dose-dependent and time-dependent induction up to 300 microM and 6 hr post-induction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus megaterium / drug effects
  • Bacterial Proteins / metabolism
  • Cytochrome P-450 Enzyme System / biosynthesis*
  • Cytochrome P-450 Enzyme System / genetics
  • Dose-Response Relationship, Drug
  • Drug Evaluation, Preclinical
  • Enzyme Induction
  • Estradiol / pharmacology*
  • Estrogens / pharmacology*
  • Genes, Reporter
  • Mixed Function Oxygenases / biosynthesis*
  • Mixed Function Oxygenases / genetics
  • NADPH-Ferrihemoprotein Reductase
  • Phenols / pharmacology*
  • Protein Binding
  • Recombinant Proteins / biosynthesis
  • Repressor Proteins / metabolism
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • Estrogens
  • Phenols
  • Recombinant Proteins
  • Repressor Proteins
  • Transcription Factors
  • 2-sec-butylphenol
  • Bm3R1 protein, Bacillus megaterium
  • Estradiol
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • NADPH-Ferrihemoprotein Reductase
  • flavocytochrome P450 BM3 monoxygenases