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The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains.
Open accessAbstract
The DNA binding activity of transcription factor AP-1 is regulated in vitro by a posttranslational mechanism involving reduction/oxidation (redox). Redox regulation is mediated by a conserved cysteine residue in the DNA-binding domain of Fos and Jun. Previously, we demonstrated that a DNA repair protein, Ref-1, could stimulate the DNA binding activity of Fos-Jun dimers by reducing this cysteine residue. To examine the relationship between the redox and repair functions of Ref-1, we generated a series of deletion mutants. Analysis of the truncated proteins in vitro revealed that the redox and repair activities are encoded by distinct regions of Ref-1. Sequences in the N-terminal domain of Ref-1 that are not present in functionally related proteins from other organisms are required for the redox activity, whereas the DNA repair activity requires conserved C-terminal sequences. Chemical alkylation or oxidation of cysteine sulfhydryls inhibits the redox activity of Ref-1 without affecting its DNA repair activity. Crosslinking studies suggest that a direct cysteine-mediated interaction occurs between Ref-1 and Jun.
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Cites
Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro
Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573
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White, B. C., Sullivan, J. M., DeGracia, D. J., O’Neil, B. J., Neumar, R. W., Grossman, L. I., Rafols, J. A., & Krause, G. S. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(00)00386-5 · Cited by 796
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Metadata
- Authors
- Xanthoudakis, S., Miao, G. G., & Curran, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-01-04
- Volume
- 91
- Issue
- 1
- Pages
- 23-27
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1972241251
- Cited by
- 354
- References
- 1
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- green
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- Xanthoudakis, S., Miao, G. G., & Curran, T. (1994). The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.1.23
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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