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Papers In Press, published online ahead of print February 4, 2004
Department of Pulmonary, University of Utah, Salt Lake City, UT 84132
Corresponding Author: john.hoidal{at}hsc.utah.edu
We previously reported that E-box and TATA-like elements repress human xanthine oxidoreductase gene (hXOR) expression. In the present investigation we determined the means by which the E-box site functions in this basal repression. DNA affinity purification demonstrated that at least five proteins are involved in the nuclear protein complex binding to the E-box and adjacent Ku86-binding sites. Amino acid sequence analysis demonstrated that three proteins, DNA-PK catalytic subunit (DNA-PKcs), Ku86 and Ku70, are components of DNA-dependent protein kinase (DNA-PK). By EMSA, gel-shift and site-directed mutagenesis we confirmed Ku86 binding to the Ku86 site. Studies indicated that the other two proteins of the complex are AREB6-like proteins binding to the E-box. Pull-down and immunoprecipitation analyses demonstrated the binding of Ku86 to AREB6-like proteins. The functional loss of Ku86 increases hXOR promoter activity and transcript expression. Based on the findings, we propose that DNA-PK/AREB6-like proteins play a central role in repression of basal hXOR activity. AREB6-like proteins specifically bind to the E-box while Ku86 binds an adjacent site and recruits DNA-PKcs and Ku70 proteins. A working model is presented to account for the role of DNA-PK and AREB6-like proteins in regulating hXOR activity.
J. Biol. Chem, 10.1074/jbc.M305856200
Submitted on June 4, 2003
Revised on February 4, 2004
Accepted on February 4, 2004
Characterization of proteins binding to E-box/Ku86 sites and function of Ku86 in transcriptional regulation of the human xanthine oxidoreductase gene
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