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J. Biol. Chem., Vol. 275, Issue 21, 15912-15916, May 26, 2000
From the Verna and Marrs McLean Department of Biochemistry and
Molecular Biology, Baylor College of Medicine,
Houston, Texas 77030
Activation domains are functional modules that
enable DNA-binding proteins to stimulate transcription.
Characterization of these essential modules in transcription factors
has been hampered by their low sequence homology. Here we delineate the
peptide sequences that are required for transactivation and interaction with hTAFII31, a classical target of the acidic class
of activation domains. Our analyses indicate that hTAFII31
recognizes a diverse set of sequences for transactivation. This
information enabled the identification of hTAFII31-binding
sequences that are critical for the activity of the activation domains
of five human transcription factors: NFAT1, ALL1, NF-IL6, ESX, and
HSF-1. The interaction surfaces are localized in short peptide segments
of activation domains. The brevity and heterogeneity of the motifs may
explain the low sequence homology among acidic activation domains.
Divergent hTAFII31-binding Motifs Hidden in
Activation Domains*,
*
This work was supported in part by research funds from
Yoshitomi Pharmaceutical Industries and the Leukemia Society of
America. The 600-MHz NMR spectrometer at the University of Houston is
funded by the W. M. Keck Foundation.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 one table.
To whom correspondence should be addressed. Fax: 713-798-1625;
E-mail: muesugi@bcm.tmc.edu.
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