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

Curt M. Horvath, George R. Stark, Ian M. Kerr, James E. Darnell*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

149 Scopus citations

Abstract

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 ~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.

Original languageEnglish (US)
Pages (from-to)6957-6964
Number of pages8
JournalMolecular and cellular biology
Volume16
Issue number12
DOIs
StatePublished - 1996

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Interactions between STAT and non-STAT proteins in the interferon- stimulated gene factor 3 transcription complex'. Together they form a unique fingerprint.

Cite this