Progesterone-binding components of chick oviduct. In vitro effect of receptor subunits on gene transcription

J Biol Chem. 1976 Sep 10;251(17):5178-86.

Abstract

We have studied chick oviduct progesterone receptor subunits and their effect on RNA transcription in oviduct chromatin. Initiation of RNA chain synthesis was measured by the rifampicin-challenge assay. Progesterone receptor subunits A and B were purified 200-fold by sequential chromatography on phosphocellulose, DEAE-cellulose, and hydroxylapatite. The subunits could be recombined to form the 6S receptor A-B dimer initially present in chick oviduct homogenates. The intact 6 S receptor dimer preparation increased transcription of oviduct chromatin by 40 to 60%. This increase corresponds to the creation of 5,800 new initiation sites per haploid cellular equivalent of DNA as chromatin. The increased chromatin transcription which resulted was half-maximal at a receptor concentration of about 5 x 10(-9) M. Preparations from other tissues which were devoid of progesterone-binding activity or oviduct preparations lacking progesterone did not stimulate rifampicin-resistant RNA synthesis. The oviduct receptor fraction contained no detectable glucocorticoid, androgen, or estrogen receptors. When isolated B subunits alone were incubated with chromatin, no transcriptional increase was detectable. Isolated A subunits increased chromatin transcription, but only at concentration approximately 10-fold higher than required of intact dimer. These observations suggest that the 6 S receptor dimer is the functional species in chromatin transcription in vivo; two hormones are required per dimer, one on each subunit. Since subunit A binds DNA and has stimulatory activity , a dimer dissociation at acceptor sites is postulated, liberating A subunits which stimulate RNA chain initiation sites.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chickens
  • Chromatin / drug effects
  • Chromatin / metabolism
  • Female
  • Kinetics
  • Manganese / pharmacology
  • Models, Biological
  • Muscle Proteins / isolation & purification
  • Muscle Proteins / metabolism*
  • Osmolar Concentration
  • Oviducts / metabolism*
  • Potassium Chloride / pharmacology
  • Progesterone / metabolism*
  • Receptors, Cell Surface* / drug effects
  • Rifampin / pharmacology
  • Transcription, Genetic* / drug effects

Substances

  • Chromatin
  • Muscle Proteins
  • Receptors, Cell Surface
  • Manganese
  • Progesterone
  • Potassium Chloride
  • Rifampin