Overproduction of full-length and truncated human estrogen receptors in Escherichia coli.

H. Ahrens, T. J. Schuh, B. L. Rainish, John Furlow, J. Gorski, G. C. Mueller

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


The full-length human estrogen receptor (hER) as well as two overlapping peptides of hER were overproduced in Escherichia coli JM109 cells, using the inducible pIC vector system. The N-terminal receptor peptide contains the DNA-binding domain as well as the hinge region, whereas the C-terminal peptide contains the same hinge region and the hormone-binding domain. Typically, 1-6 mg of estrogen receptor (ER) peptides can be recovered from 1 L E. coli cell cultures. The majority of the overexpressed proteins are found in inclusion bodies, which allow the isolation of ER peptides in high yields and of 50-80% purity. Induction for short time periods at 10 microM inducer yielded up to 50% of the ER peptides in soluble form with full biological activity. Both the intact receptor and the C-terminal fragment specifically bound estrogens and antiestrogens, whereas ER peptides that contained the DNA-binding domain were retained on a DNA-agarose resin.

Original languageEnglish (US)
Pages (from-to)77-92
Number of pages16
Issue number2
StatePublished - Jun 1 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology


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