A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain

C. M. Horvath*, Z. Wen, J. E. Darnell

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

438 Scopus citations

Abstract

Stat1 and Stat3 are two members of the ligand-activated transcription factor family that serve the dual functions of signal transducers and activators of transcription. Whereas the two proteins select very similar (not identical) optimum binding sites from random oligonucleotides, differences in their binding affinity were readily apparent with natural STAT-binding sites. To take advantage of these different affinities, chimeric Stat1:Stat3 molecules were used to locate the amino acids that could discriminate a general binding site from a specific binding site. The amino acids between residues ~400 and ~500 of these ~750-amino-acid-long proteins determine the DNA-binding site specificity. Mutations within this region result in Stat proteins that are activated normally by tyrosine phosphorylation and that dimerize but have greatly reduced DNA-binding affinities.

Original languageEnglish (US)
Pages (from-to)984-994
Number of pages11
JournalGenes and Development
Volume9
Issue number8
DOIs
StatePublished - Apr 15 1995

Keywords

  • DNA binding
  • STAT proteins
  • site selection

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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