Nuclear estrogen receptor II (nER-II) is involved in the estrogen-dependent ribonucleoprotein transport in the goat uterus: II. Isolation and characterization of three small nuclear ribonucleoprotein proteins which bind to nER-II

J Cell Biochem. 2002;84(2):227-36. doi: 10.1002/jcb.1280.

Abstract

Three proteins of a goat uterine small nuclear ribonucleoprotein (snRNP) fraction, which bind to nuclear estrogen receptor-II (nER-II) have been isolated and purified. These are the p32, p55, and p60 of which p32 is the major nER-II binding protein. Indirect evidence reveals that p32 binds to the nuclear export signal (NES) on the nER-II. nER-II is a snRNA binding protein while p32 does not bind to the RNA. nER-II along with p32 and p55 form an effective Mg(++)ATPase complex, the activation of which appears to be the immediate reason behind the RNP exit from the nuclei following estradiol exposure. The three nER-II binding proteins bind to the nuclear pore complex; nER-II does not possess this property.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Goats
  • Protein Binding
  • Protein Transport
  • Receptors, Estrogen / metabolism
  • Receptors, Estrogen / physiology*
  • Ribonucleoproteins, Small Nuclear / isolation & purification*
  • Ribonucleoproteins, Small Nuclear / metabolism

Substances

  • Receptors, Estrogen
  • Ribonucleoproteins, Small Nuclear
  • Adenosine Triphosphatases