Skip to main content

Multiple proteins interact with the nuclear inhibitory protein repressor element in the human interleukin-3 promoter.

Publication ,  Journal Article
Engeland, K; Andrews, NC; Mathey-Prevot, B
Published in: J Biol Chem
October 13, 1995

T cell expression of interleukin 3 (IL-3) is directed by positive and negative cis-acting DNA elements clustered within 300 base pairs of the transcriptional start site. A strong repressor element, termed nuclear inhibitory protein (NIP), was previously mapped to a segment of the IL-3 promoter between nucleotides -271 and -250. Functional characterization of this element demonstrates that it can mediate repression when linked in cis to a heterologous promoter. DNA binding experiments were carried out to characterize the repressor activity. Using varying conditions, three distinct complexes were shown to interact specifically with the NIP region, although only one correlates with repressor activity. Complex 1 results from binding of a ubiquitous polypeptide that recognizes the 3' portion of this sequence and is not required for repression. Complex 2 corresponds to binding of transcription factor (upstream stimulatory factor) to an E-box motif in the 5' portion of the NIP region. DNA binding specificity of complex 3 overlaps with that of upstream stimulatory factor but is clearly distinct. To determine which of the latter two complexes represents NIP activity, we incorporated small alterations into the NIP site of an IL-3 promoter-linked reporter construct and examined their effects on NIP-mediated repression. Functional specificity for repression matches the DNA binding specificity of complex 3; both repressor activity and complex 3 binding require the consensus sequence CTCACNTNC.

Duke Scholars

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

October 13, 1995

Volume

270

Issue

41

Start / End Page

24572 / 24579

Location

United States

Related Subject Headings

  • Transfection
  • T-Lymphocytes
  • Restriction Mapping
  • Repressor Proteins
  • Recombinant Proteins
  • Promoter Regions, Genetic
  • Oligonucleotide Probes
  • Molecular Sequence Data
  • Interleukin-3
  • Hylobates
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Engeland, K., Andrews, N. C., & Mathey-Prevot, B. (1995). Multiple proteins interact with the nuclear inhibitory protein repressor element in the human interleukin-3 promoter. J Biol Chem, 270(41), 24572–24579. https://doi.org/10.1074/jbc.270.41.24572
Engeland, K., N. C. Andrews, and B. Mathey-Prevot. “Multiple proteins interact with the nuclear inhibitory protein repressor element in the human interleukin-3 promoter.J Biol Chem 270, no. 41 (October 13, 1995): 24572–79. https://doi.org/10.1074/jbc.270.41.24572.
Engeland K, Andrews NC, Mathey-Prevot B. Multiple proteins interact with the nuclear inhibitory protein repressor element in the human interleukin-3 promoter. J Biol Chem. 1995 Oct 13;270(41):24572–9.
Engeland, K., et al. “Multiple proteins interact with the nuclear inhibitory protein repressor element in the human interleukin-3 promoter.J Biol Chem, vol. 270, no. 41, Oct. 1995, pp. 24572–79. Pubmed, doi:10.1074/jbc.270.41.24572.
Engeland K, Andrews NC, Mathey-Prevot B. Multiple proteins interact with the nuclear inhibitory protein repressor element in the human interleukin-3 promoter. J Biol Chem. 1995 Oct 13;270(41):24572–24579.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

October 13, 1995

Volume

270

Issue

41

Start / End Page

24572 / 24579

Location

United States

Related Subject Headings

  • Transfection
  • T-Lymphocytes
  • Restriction Mapping
  • Repressor Proteins
  • Recombinant Proteins
  • Promoter Regions, Genetic
  • Oligonucleotide Probes
  • Molecular Sequence Data
  • Interleukin-3
  • Hylobates