Journal article
Redox modulation of AP-2 DNA binding activity in vitro
Biochemical and biophysical research communications, Vol.249(2), pp.307-312
08/19/1998
DOI: 10.1006/bbrc.1998.9139
PMID: 9712692
Abstract
Transcription factor AP-2 plays a critical role in regulating gene expression during vertebrate development and cellular differentiation. We report here that AP-2 DNA binding in vitro can be reversibly modulated by redox conditions and that thioredoxin is a potent stimulator of AP-2 DNA binding. Our studies indicate that oxidation of recombinant human AP-2 with diamide or hydrogen peroxide inhibits its DNA binding activity to synthetic AP-2 oligodeoxynucleotides. The inhibitory effect of diamide on AP-2 DNA binding was dose-dependent and was reversible by addition of reducing agents beta-mercaptoethanol, dithiothreitol, and thioredoxin. Immunoblot assays indicated that treatment with oxidants caused a change in migration of the AP-2 protein in nonreducing gels and that this effect was also reversible by treatment of the oxidized AP-2 with reducing agents. These data suggest a mechanism by which the oxidation state of conserved cysteine residues in the AP-2 DNA binding domain may contribute to its DNA binding activity. AP-2 joins a group of other transcription factors whose functions are regulated in part by their redox states.
Details
- Title: Subtitle
- Redox modulation of AP-2 DNA binding activity in vitro
- Creators
- Yuanhui Huang - Radiation and Free Radical Biology Graduate Program, University of Iowa, Iowa City, Iowa, 52242, USAFrederick E Domann
- Resource Type
- Journal article
- Publication Details
- Biochemical and biophysical research communications, Vol.249(2), pp.307-312
- Publisher
- United States
- DOI
- 10.1006/bbrc.1998.9139
- PMID
- 9712692
- ISSN
- 0006-291X
- eISSN
- 1090-2104
- Grant note
- CA73612 / NCI NIH HHS
- Language
- English
- Date published
- 08/19/1998
- Academic Unit
- Pathology; Surgery; Radiation Oncology
- Record Identifier
- 9984047609602771
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