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Originally published In Press as doi:10.1074/jbc.M011582200 on January 17, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16207-16215, May 11, 2001
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DNA Binding by the ETS-domain Transcription Factor PEA3 Is Regulated by Intramolecular and Intermolecular Protein·Protein Interactions*

Amanda GreenallDagger , Nicola WillinghamDagger , Ed Cheung§, David S. Boam§, and Andrew D. SharrocksDagger §

From the Dagger  School of Biochemistry and Genetics, The Medical School, University of Newcastle Upon Tyne, Newcastle Upon Tyne NE2 4HH and the § School of Biological Sciences, University of Manchester, 2.205 Stopford Bldg., Oxford Road, Manchester M13 9PT, United Kingdom

The control of DNA binding by eukaryotic transcription factors represents an important regulatory mechanism. Many transcription factors are controlled by cis-acting autoinhibitory modules that are thought to act by blocking promiscuous DNA binding in the absence of appropriate regulatory cues. Here, we have investigated the determinants and regulation of the autoinhibitory mechanism employed by the ETS-domain transcription factor, PEA3. DNA binding is inhibited by a module composed of a combination of two short motifs located on either side of the ETS DNA-binding domain. A second type of protein, Ids, can act in trans to mimic the effect of these cis-acting inhibitory motifs and reduce DNA binding by PEA3. By using a one-hybrid screen, we identified the basic helix-loop-helix-leucine zipper transcription factor USF-1 as an interaction partner for PEA3. PEA3 and USF-1 form DNA complexes in a cooperative manner. Moreover, the formation of ternary PEA3·USF-1·DNA complexes requires parts of the same motifs in PEA3 that form the autoinhibitory module. Thus the binding of USF-1 to PEA3 acts as a switch that modifies the autoinhibitory motifs in PEA3 to first relieve their inhibitory action, and second, promote ternary nucleoprotein complex assembly.

* This work was supported by grants from the Biotechnology and Biological Sciences and Research Council (GR/H09676 to D. B.) and from the Cancer Research Campaign (CRC) and a Lister Institute of Preventative Medicine Research Fellowship (to A.D.S.).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.

To whom correspondence should be addressed: Tel.: 44-161-275-5979; Fax: 44-161-275-5082; E-mail: a.d.sharrocks@man.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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