Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Interactions between STAT and non-STAT proteins in the interferon-stimulated gene factor 3 transcription complex.

http://www.ncbi.nlm.nih.gov/pubmed/8943351

The first STAT-containing transcription factor to be studied, the alpha-interferon-induced ISGF3, is composed of a Stat1:2 heterodimer and a weak DNA-binding protein, p48, that is a member of a growing family of proteins similar to the so-called interferon regulatory factor (IRF-1). The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA, but we show that amino acids approximately 150 to 250 of Stat1 and a COOH-terminal portion of p48 exhibit physical interaction, implying contact that stabilizes ISGF3. Moreover, amino acid exchanges within the Stat1 contact region diminish or abolish the functional activity of Stat1. This protein interaction domain may be important in other STAT proteins to recruit partners to multiprotein transcription factors.

Pubmed ID: 8943351 RIS Download

Mesh terms: DNA-Binding Proteins | Interferon-Stimulated Gene Factor 3 | Interferon-Stimulated Gene Factor 3, gamma Subunit | Protein Binding | STAT1 Transcription Factor | STAT2 Transcription Factor | Trans-Activators | Transcription Factors | Transcription, Genetic

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIAID NIH HHS, Id: AI32489
  • Agency: NIAID NIH HHS, Id: AI34420

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.