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Molecular and Cellular Biology, March 1999, p. 2231-2241, Vol. 19, No. 3
Division of Basic Immunology, Department of
Medicine, National Jewish Medical and Research Center, Denver, Colorado
802061; Department of
Immunology2 and Cancer
Center,3 University of Colorado Health Sciences
Center, Denver, Colorado 80262; and Department of Biochemistry
and Molecular Biology, and Department of Chemistry, University of
British Columbia, Vancouver, British Columbia V6T 1Z3,
Canada4
Received 19 August 1998/Returned for modification 14 October
1998/Accepted 11 November 1998
Pax family transcription factors bind DNA through the paired
domain. This domain, which is comprised of two helix-turn-helix motifs
and a
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Highly Conserved
-Hairpin of the Paired
DNA-Binding Domain Is Required for Assembly of Pax-Ets Ternary
Complexes

-hairpin structure, is a target of mutations in congenital
disorders of mice and humans. Previously, we showed that Pax-5
(B-cell-specific activator protein) recruits proteins of the Ets
proto-oncogene family to bind a composite DNA site that is essential
for efficient transcription of the early-B-cell-specific mb-1 promoter. Here, evidence is provided for specific
interactions between Ets-1 and the amino-terminal subdomains of Pax
proteins. By tethering deletion fragments of Pax-5 to a heterologous
DNA-binding domain, we show that 73 amino acids (amino acids 12 to 84)
of its amino-terminal subdomain can recruit the ETS domain of Ets-1 to
bind the composite site. Furthermore, an amino acid (Gln22) within the
highly conserved
-hairpin motif of Pax-5 is essential for efficient
recruitment of Ets-1. The ability to recruit Ets proteins to bind DNA
is a shared property of Pax proteins, as demonstrated by cooperative
DNA binding of Ets-1 with sequences derived from the paired domains of
Pax-2 and Pax-3. The strict conservation of sequences required for
recruitment of Ets proteins suggests that Pax-Ets interactions are
important for regulating transcription in diverse tissues during
cellular differentiation.
*
Corresponding author. Mailing address: Division of
Basic Immunology, National Jewish Medical and Research Center, 1400 Jackson St., K516B, Denver, CO 80206. Phone: (303) 398-1398. Fax: (303) 398-1396. E-mail: hagmanj{at}njc.org.
Present address: Department of Life Sciences, University of New
England, Biddeford, ME 04005.
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