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Two distinct cellular phosphoproteins bind to the c-fos serum response element
W A Ryan1, B R Franza, M Z Gilman
1Cold Spring Harbor Laboratory, NY 11724.
The EMBO Journal
|June 1, 1989
Summary
Researchers discovered a second protein that binds to the serum response element (SRE), suggesting distinct proteins mediate the SRE's multiple functions in gene regulation.
Area of Science:
- Molecular Biology
- Gene Regulation
- Transcription Factors
Background:
- Serum growth factors induce c-fos transcription via a specific DNA sequence, the serum response element (SRE).
- The SRE is known as a binding site for the nuclear protein serum response factor (SRF).
- Direct evidence linking SRF activity to SRE function is lacking.
Purpose of the Study:
- To investigate the binding proteins of the serum response element (SRE).
- To determine if other proteins besides serum response factor (SRF) bind to the SRE.
- To explore the potential for distinct proteins mediating SRE functions.
Main Methods:
- Characterization of SRE-binding proteins using size and chromatographic properties.
- Assessment of binding specificity and nucleotide contact points within the SRE.
- Analysis of cellular extracts for the presence of distinct SRE-binding proteins.
Main Results:
- A second, distinct SRE-binding protein was identified in cells.
- This novel protein differs from SRF in size, chromatographic behavior, and binding specificity.
- The new protein makes unique contacts with nucleotides within the SRE sequence.
Conclusions:
- Cells possess at least two distinct proteins capable of binding to the SRE.
- These distinct SRE-binding proteins may independently mediate the SRE's diverse functions.
- This finding provides a molecular basis for the complex roles of the SRE in gene expression.