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Altered protein conformation on DNA binding by Fos and Jun
1Department of Molecular Oncology & Virology, Roche Institute of Molecular Biology, Nutley, New Jersey 07110.
Nature
|October 11, 1990
Summary
The Fos and Jun proteins form a complex that regulates gene transcription. New methods show this complex changes shape and increases alpha-helical content upon binding DNA, clarifying protein-DNA interactions.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- The c-fos and c-jun proto-oncogenes encode Fos and Jun proteins, which form heterodimers.
- This Fos-Jun complex binds to the activator protein-1 (AP-1) site, regulating gene transcription.
- Previous studies on Fos-Jun dimerization and DNA binding relied on indirect methods.
Purpose of the Study:
- To develop direct assay systems for monitoring Fos-Jun dimerization and DNA binding.
- To elucidate the precise nature of the protein-DNA interaction between Fos-Jun dimers and the AP-1 site.
Main Methods:
- Development of novel assay systems.
- Utilizing fluorescence spectroscopy to monitor dimerization and DNA binding.
- Employing circular dichroism to analyze protein conformation changes.
Main Results:
- Direct monitoring of Fos-Jun dimerization and DNA binding was achieved.
- The interaction of Fos and Jun proteins with DNA induced an altered conformation of the protein dimers.
- An increase in alpha-helical content was observed upon DNA binding.
Conclusions:
- The study provides direct evidence of conformational changes in Fos-Jun dimers upon DNA interaction.
- Developed fluorescence spectroscopy and circular dichroism techniques offer a general approach for studying transcriptional regulatory protein-DNA interactions.
- These findings enhance understanding of gene transcription regulation by Fos-Jun complex.
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