An orphan nuclear receptor lacking a zinc-finger DNA-binding domain: interaction with several nuclear receptors

Biochim Biophys Acta. 1997 Jan 3;1350(1):27-32. doi: 10.1016/s0167-4781(96)00196-0.

Abstract

The yeast two-hybrid screening was applied to cloning cDNAs of proteins that interact with peroxisome proliferator-activated receptor alpha (PPAR alpha). We obtained from a rat liver cDNA library a clone encoding a protein related to the ligand-binding domain of the members of nuclear hormone receptor superfamily, whereas apparently lacking the zinc-finger DNA-binding domain. This protein interacted with the activated forms of several nuclear receptors, and thus is a novel type of heterodimer-forming nuclear receptor.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism
  • Gene Library
  • Humans
  • Liver / metabolism*
  • Molecular Sequence Data
  • Organ Specificity
  • Rats
  • Receptors, Cytoplasmic and Nuclear / chemistry
  • Receptors, Cytoplasmic and Nuclear / genetics*
  • Receptors, Cytoplasmic and Nuclear / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Restriction Mapping
  • Sequence Homology, Amino Acid
  • Transcription Factors / chemistry
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism
  • Zinc Fingers

Substances

  • DNA, Complementary
  • DNA-Binding Proteins
  • Receptors, Cytoplasmic and Nuclear
  • Recombinant Proteins
  • Transcription Factors

Associated data

  • GENBANK/D86580
  • GENBANK/D86745
  • GENBANK/D86839