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Originally published In Press as doi:10.1074/jbc.C000484200 on August 8, 2000

J. Biol. Chem., Vol. 275, Issue 40, 30801-30805, October 6, 2000
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Functional Interaction between the p160 Coactivator Proteins and the Transcriptional Enhancer Factor Family of Transcription Factors*

Borja BelandiaDagger and Malcolm G. Parker§

From the Molecular Endocrinology Laboratory, Imperial Cancer Research Fund,London WC2A 3PX, United Kingdom

SRC1, initially identified as a nuclear receptor coactivator, was found to interact with a member of the transcriptional enhancer factor (TEF) family of transcription factors, TEF-4. The interaction, which occurs in both intact cells and in a cell-free system, is mediated by the highly conserved basic helix-loop-helix/Per-Arnt-Sim (bHLH-PAS) domain present in the N-terminal region of SRC1. Moreover, all three members of the p160 family of nuclear receptor coactivators, SRC1, TIF2, and RAC3, are able to potentiate transcription from a TEF response element in transient transfection experiments, and this activation requires the presence of the bHLH-PAS domain. These results suggest that the p160 proteins could be bona fide coactivators of the TEF family of transcription factors.


* This work was supported by the Imperial Cancer Research Fund.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.

Dagger Supported by the European Community Training and Mobility of Researchers program.

§ To whom correspondence should be addressed. Tel.: 44-20-7269-3280; Fax: 44-20-7269-3094; E-mail: m.parker@icrf.icnet.uk.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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