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Volume 271, Number 41, Issue of October 11, 1996 pp. 25617-25623
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Redox Regulation of GA-binding Protein-alpha DNA Binding Activity

(Received for publication, January 17, 1996, and in revised form, July 23, 1996)

Mark E. Martin , Yurii Chinenov , Mi Yu , Tonya K. Schmidt and Xiu-Ying Yang

From the Department of Biochemistry, University of Missouri, Columbia, Missouri 65212

We have investigated the reduction/oxidation (redox) regulation of the heteromeric transcription factor GA-binding protein (GABP). GABP, also known as nuclear respiratory factor 2, regulates the expression of nuclear encoded mitochondrial proteins involved in oxidative phosphorylation, including cytochrome c oxidase subunits IV and Vb, as well as the expression of mitochondrial transcription factor 1. GABP is composed of two subunits, the Ets-related GABP-alpha , which mediates specific DNA binding, and GABP-beta , which forms heterodimers and heterotetramers on DNA sequences containing the PEA3/Ets motif ((C/A)GGA(A/T)(G/A)). We demonstrate here that GABP DNA binding activity and GABP-dependent gene expression in 3T3 cells are inhibited by pro-oxidant conditions. DNA binding of recombinant GABP-alpha was activated by chemical reduction (dithiothreitol) and by thioredoxin; however, GSSG inhibited GABP DNA binding activity. Treatment of GABP-alpha , but not GABP-beta 1, with sulfhydryl-alkylating agents also inhibited GABP DNA binding activity. Our results suggest that GABP DNA binding activity is redox-regulated in vivo, possibly by thioredoxin-mediated reduction and by GSSG-mediated oxidation of the GABP-alpha subunit. The regulation of GABP (nuclear respiratory factor 2) DNA binding activity by cellular redox changes provides an important link between mitochondrial and nuclear gene expression and the redox state of the cell.


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