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Volume 272, Number 14, Issue of April 4, 1997 pp. 9344-9355
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Identification and Characterization of TF1^phox, a DNA-binding Protein That Increases Expression of gp91^phox in PLB985 Myeloid Leukemia Cells

(Received for publication, August 14, 1996, and in revised form, January 22, 1997)

From the Lurleen B. Wallace Tumor Institute, Department of Hematology and Oncology, and the Comprehensive Cancer Center, University of Alabama, Birmingham School of Medicine, Birmingham, Alabama 35294

The CYBB gene encodes gp91^phox, the heavy chain of the phagocyte-specific NADPH oxidase. CYBB is transcriptionally inactive until the promyelocyte stage of myelopoiesis, and in mature phagocytes, expression of gp91^phox is further increased by interferon- (IFN-) and other inflammatory mediators. The CYBB promoter region contains several lineage-specific cis-elements involved in the IFN- response. We screened a leukocyte cDNA expression library for proteins able to bind to one of these cis-elements (214 to 262 base pairs) and identified TF1^phox, a protein with sequence-specific binding to the CYBB promoter. Electrophoretic mobility shift assay with nuclear proteins from a variety of cell lines demonstrated binding of a protein to the CYBB promoter that was cross-immunoreactive with TF1^phox. DNA binding of this protein was increased by IFN- treatment in the myeloid cell line PLB985, but not in the non-myeloid cell line HeLa. Overexpression of recombinant TF1^phox in PLB985 cells increased endogenous gp91^phox message abundance, but did not lead to cellular differentiation. Overexpression of TF1^phox in myeloid leukemia cell lines increased reporter gene expression from artificial promoter constructs containing CYBB promoter sequence. These data suggested that TF1^phox increased expression of gp91^phox.

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