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J. Biol. Chem., Vol. 276, Issue 43, 40127-40132, October 26, 2001
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From the Department of Natural Sciences, Södertörns
högskola, Box 4101, S-14104 Huddinge, Sweden and the Centers for
The product of the proto-oncogene
c-myc influences many cellular processes through the
regulation of specific target genes. Through its transactivation domain
(TAD), c-Myc protein interacts with several transcription factors,
including TATA-binding protein (TBP). We present data that suggest that
in contrast to some other transcriptional activators, an extended
length of the c-Myc TAD is required for its binding to TBP. Our data
also show that this interaction is a multistep process, in which a
rapidly forming low affinity complex slowly converts to a more stable
form. The initial complex formation results from ionic or polar
interactions, whereas the slow conversion to a more stable form is
hydrophobic in nature. Based on our results, we suggest two alternative
models for activation domain/target protein interactions, which
together provide a single universal paradigm for understanding
activator-target factor interactions.
How Transcriptional Activators Bind Target Proteins*
§,
Biotechnology and ¶ Structural Biochemistry,
Department of Biosciences, Karolinska Institutet, NOVUM, S-14157
Huddinge, Sweden
*
This work was supported by a grant from the Swedish Natural
Science Research Council and by the Swedish Cancer Society.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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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