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Behind the Fos and Jun leucine zipper
1Department of Biochemistry, Kaplan Cancer Center, N.Y. University Medical Center, New York 10016.
Cancer Cells (Cold Spring Harbor, N.Y. : 1989)
|November 1, 1989
Summary
Nuclear oncoproteins Fos and Jun form a complex that binds DNA and activates gene transcription. This suggests Fos and Jun are part of a larger network of related transcription factors.
Area of Science:
- Molecular Biology
- Cellular Biology
- Genetics
Background:
- Nuclear oncoproteins Fos and Jun are rapidly induced by extracellular signals.
- These proteins form a heterodimer complex in the nucleus through leucine zipper domains.
Purpose of the Study:
- To investigate the DNA binding and transcriptional activation properties of the Fos-Jun complex.
- To explore the potential network of related transcription factors.
Main Methods:
- Analysis of protein-protein interactions (leucine zipper domains).
- DNA binding assays using the TPA-responsive element (TRE).
- Assessment of transcriptional activation of TPA-responsive genes.
Main Results:
- The Fos-Jun heterodimer binds to the TPA-responsive element (TRE) via a basic motif.
- This complex activates the transcription of TPA-responsive genes.
- Related Fos and Jun proteins exhibit similar dimerization and DNA binding properties.
Conclusions:
- Fos and Jun form a functional transcription factor complex.
- These oncoproteins are likely part of a broader network of related transcription factors.