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J. Biol. Chem., Vol. 276, Issue 9, 6675-6688, March 2, 2001
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From the 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
(N4) was confirmed, but analysis of weak binding
sites showed that STAT6 binds fairly well to N3 sites. As
previously reported, STAT1 and STAT5 prefer N3 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.
DNA Binding Specificity of Different STAT
Proteins
COMPARISON OF IN VITRO SPECIFICITY WITH
NATURAL TARGET SITES*,
§¶,,
,§§,, and
Swiss Institute for Experimental Cancer
Research (ISREC) 1066 Epalinges, Switzerland, Tularik Inc.,
South San Francisco, California 94080, ** Mount Sinai School of
Medicine, Immunobiology Center, New York, New York 10029-6574, and the Institute for Microbiology,
Biochemistry and Genetics, University of Erlangen-Nürnberg,
D-91058 Erlangen, Germany
*
This work was supported in part by research grants from the
Swiss National Science Foundation (to M. N.) and from the Deutsche Forschungsgemeinschaft Grant DFG SFB 473, project B6 (to G. Fey at the
University Erlangen-Nürnberg).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains sequences selected by STAT1,
STAT5A, and STAT6, and Fig. 5.
§
Present address Universität Heidelberg, Im Neuenheimer Feld
346, D-69120 Heidelberg, Germany.
¶
To whom correspondence should be addressed. Tel.:
41-21-692-58-92; Fax: 41-21-652-6933; E-mail:
markus.nabholz@isrec.unil.ch.
§§
Present address: NanoTools GmbH, Tscheulinstrasse 21, D-79331
Teningen, Germany.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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