DNA binding specificity of different STAT proteins: Comparison of in vitro specificity with natural target sites

Georg B. Ehret, Patrick Reichenbach, Ulrike Schindler, Curt M. Horvath, Stefan Fritz, Markus Nabholz, Philipp Bucher

Research output: Contribution to journalArticlepeer-review

300 Scopus citations


STAT transcription factors are expressed in many cell types and bind to similar sequences. However, different STAT gene knock-outs show very distinct phenotypes. To determine whether differences between the binding specificities of STAT proteins account for these effects, we compared the sequences bound by STAT1, STAT5A, STAT5B, and STAT6. One sequence set was selected from random oligonucleotides by recombinant STAT1, STAT5A, or STAT6. For another set including many weak binding sites, we quantified the relative affinities to STAT1, STAT5A, STAT5B, and STAT6. We compared the results to the binding sites in natural STAT target genes identified by others. The experiments confirmed the similar specificity of different STAT proteins. Detailed analysis indicated that STAT5A specificity is more similar to that of STAT6 than that of STAT1, as expected from the evolutionary relationships. The preference of STAT6 for sites in which the half-palindromes (TTC) are separated by four nucleotides (N 4) was confirmed, but analysis of weak binding sites showed that STAT6 binds fairly well to N3 sites. As previously reported, STAT1 and STAT5 prefer N8 sites; however, STAT5A, but not STAT1, weakly binds N4 sites. None of the STATs bound to half-palindromes. There were no specificity differences between STAT5A and STAT5B.

Original languageEnglish (US)
Pages (from-to)6675-6688
Number of pages14
JournalJournal of Biological Chemistry
Issue number9
StatePublished - Mar 2 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'DNA binding specificity of different STAT proteins: Comparison of in vitro specificity with natural target sites'. Together they form a unique fingerprint.

Cite this