| Autor: |
Jeremy H. Lakey, Yan Ling, E. C. Roberts, Andrew D. Sharrocks, Adam G. West |
| Rok vydání: |
1998 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 273:10506-10514 |
| ISSN: |
0021-9258 |
| DOI: |
10.1074/jbc.273.17.10506 |
| Popis: |
Serum response elements (SREs) play important roles in transforming extracellular signals into specific nuclear responses. The SRE-binding protein, serum response factor (SRF), plays a pivotal role in this process. Several transcription factors have been shown to interact with SRF and thereby create distinct complexes with different regulatory potentials. The ETS domain transcription factor Elk-1 is one such protein and serves to integrate distinct mitogen-activated protein kinase cascades at SREs. Elk-1 uses a short hydrophobic surface presented on the surface of an alpha-helix to interact with SRF. In this study we have used site-directed mutagenesis to identify residues in SRF that comprise the Elk-1 binding surface. The Elk-1 binding surface is composed of residues that lie on a hydrophobic surface-exposed groove located at the junction of the MADS box and C-terminal SAM motif. Different residues are implicated in interactions between SRF and the transcription factor Fli-1, indicating that although some overlap with the Elk-1 binding surface occurs, their interaction surfaces on SRF are distinct. Our data are consistent with the hypothesis that the SRF DNA-binding domain acts as docking site for multiple transcription factors that can bind to small surface-exposed patches within this domain. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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