Protein-protein interaction between the transcriptional repressor E4BP4 and the TBP-binding protein Dr1

Nucleic Acids Res. 1996 Sep 15;24(18):3607-13. doi: 10.1093/nar/24.18.3607.

Abstract

We have previously mapped a repression domain from the active transcriptional repressor E4BP4 to a 65 amino acid segment near the C-terminus of the polypeptide. Here we show that the E4BP4 repression domain interacts specifically with the TBP binding repressor protein Dr1. Mutants that affect the ability of E4BP4 to bring about transcriptional repression are also deficient in their binding of Dr1. The results are discussed in the light of evidence for squelching of a 'global' repressor by a DNA binding defective E4BP4 mutant.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenovirus E1A Proteins / metabolism
  • Amino Acid Sequence
  • Basic-Leucine Zipper Transcription Factors
  • DNA Polymerase II / metabolism
  • DNA-Binding Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • G-Box Binding Factors
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Phosphoproteins / metabolism*
  • Plasmids / metabolism
  • Protein Binding
  • Repressor Proteins / metabolism*
  • Saccharomyces cerevisiae
  • Sequence Alignment
  • Sodium Chloride / pharmacology
  • Transcription Factors / metabolism*
  • Transcription, Genetic

Substances

  • Adenovirus E1A Proteins
  • Basic-Leucine Zipper Transcription Factors
  • DNA-Binding Proteins
  • G-Box Binding Factors
  • NFIL3 protein, human
  • Phosphoproteins
  • Repressor Proteins
  • Transcription Factors
  • down-regulator of transcription 1
  • Sodium Chloride
  • DNA Polymerase II