Purification of a nuclear protein (Receptor Binding Factor-1) associated with the chromatin acceptor sites for the avian oviduct progesterone receptor

John Rejman, James Landers, Amy Goldberger, Daniel J. McCormick, Barbara Gosse, T. C. Spelsberg

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

The specific high affinity binding of the avian oviduct progesterone receptor (PR) to target cell nuclei and chromatin has been shown to involve DNA complexed with specific chromatin acceptor proteins. One of these chromatin acceptor proteins has been partially purified and found to be a small hydrophobic protein with a broad pI of 5.0-6.0 [Goldberger and Spelsberg (1988), Biochem.27, 2103-2109]. Using western immunoblots with anti-RBF-1 polyclonal antibodies to monitor the purification, a 10 kD candidate acceptor protein, termed the Receptor Binding Factor-1 (RBF-1), has been purified to apparent homogeneity. RBF-1 has an amino acid composition consistent with a hydrophobic protein having an acidic pI and a unique N-terminal sequence. Two-dimensional polyacrylamide gel electrophoresis and high-performance capillary electrophoresis support the purity of a protein ≊10 kD in size, having an acidic pI, but with evidence of several differently charged isoforms. Phosphatase treatment provides evidence that charge heterogeneity may result from variable phosphorylation states. A role of this factor as a candidate "acceptor protein" in the chromatin acceptor sites for the avian oviduct PR is proposed.

Original languageEnglish (US)
Pages (from-to)651-667
Number of pages17
JournalJournal of Protein Chemistry
Volume10
Issue number6
DOIs
StatePublished - Dec 1 1991

Keywords

  • Progesterone receptor binding factor
  • acceptor sites
  • chromatin

ASJC Scopus subject areas

  • Biochemistry

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