Components of a stat recognition code: Evidence for two layers of molecular selectivity

Ulrike Schindler, Pengguang Wu, Mike Rothe, Mike Brasseur, Steven L. McKnight

Research output: Contribution to journalArticlepeer-review

226 Scopus citations

Abstract

Latent and activated forms of Stat1 and Stat6 have been expressed and purified, enabling biochemical experiments relating to their functional activities. Stat1 bound to a phosphotyrosine peptide derived from the IFNγ receptor with a KD of 50 nM, whereas Stat6 bound to an IL-4 receptor peptide with a KD of 300 nM. Stat-receptor peptide interactions were specific and dependent upon tyrosine phosphorylation. Activated forms of Stat1 and Stat6 were used to select their optimal DNA binding sites. Stat1 selected a recognition site having dyad half-sites separated by 3 bp. Stat6 selected a recognition site composed of the same dyad half-sites, yet separated by 4 bp. Chimeric Stat1-Stat6 recombinants were expressed, purified, and assayed for receptor coupling and DNA binding specificity. Such studies led to the Identification of polypeptide domains that specify these activities. These observations provide a framework for understanding how different cytokines elicit distinctive patterns of gene expression.

Original languageEnglish (US)
Pages (from-to)689-697
Number of pages9
JournalImmunity
Volume2
Issue number6
DOIs
StatePublished - Jun 1995

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

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