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Mol Cell Biol, April 1998, p. 2252-2261, Vol. 18, No. 4
Howard Hughes Medical Institute, University
of California, Berkeley, California 94720
Received 28 October 1997/Returned for modification 7 January
1998/Accepted 27 January 1998
Adf-1 is an essential Drosophila melanogaster
sequence-specific transactivator that binds the promoters of a diverse
group of genes. We have performed a comprehensive mapping of the
functional domains of Adf-1 to study the role of transactivators in the
process of gene activation. Using a series of clustered point mutations and small deletions we have identified regions of Adf-1 required for
DNA binding, dimerization, and activation. In contrast to most
enhancer-binding factors, the Adf-1 activation regions are nonmodular
and depend on an intact protein, including the Adf-1 DNA-binding
domain, for activity. Like many transcriptional activators, Adf-1
contains a TFIID-binding domain that can interact with specific TAF
subunits. Although TAFs are required for Adf-1-directed activation, TAF
binding is not sufficient, suggesting that Adf-1 may direct multiple
essential steps during activation. Interestingly, both the TAF-binding
domain and the DNA-binding domain contain sequences homologous to those
of the Myb family of DNA-binding domains. Thus, Adf-1 has evolved an
unusual structure containing two versions of the Myb motif, one that
binds DNA and one that binds proteins.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Adf-1 Is a Nonmodular Transcription Factor That
Contains a TAF-Binding Myb-Like Motif

*
Corresponding author. Mailing address: Molecular and
Cell Biology, 401 Barker Hall Mailroom, University of California,
Berkeley, CA 94720-3204. Phone: (510) 642-0884. Fax: (510) 643-9547. E-mail: jmlim{at}uclink4.berkeley.edu.
Present address: Tulerik Inc., South San Francisco, Calif.
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