@article {4696,
	title = {The highly conserved beta-hairpin of the paired DNA-binding domain is required for assembly of Pax-Ets ternary complexes},
	journal = {Molecular and Cellular Biology},
	volume = {19},
	number = {3},
	year = {1999},
	note = {ISI Document Delivery No.: 168MYTimes Cited: 37Cited Reference Count: 57},
	month = {Mar},
	pages = {2231-2241},
	type = {Article},
	abstract = {Pax family transcription factors bind DNA through the paired domain. This domain, which is comprised of two helix-turn-helix motifs and a beta-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 beta-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.},
	keywords = {B-CELL-DEVELOPMENT, BOX, GENE, HMG DOMAIN, MURINE ETS-1, POINT MUTATION, STRUCTURAL BASIS, TRANSCRIPTION FACTORS, V-ETS, WAARDENBURG-SYNDROME},
	isbn = {0270-7306},
	url = {<Go to ISI>://000078697900061},
	author = {Wheat, W. and Fitzsimmons, D. and Lennox, H. and Krautkramer, S. R. and Gentile, L. N. and McIntosh, L. P. and Hagman, J.}
}
