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Interaction of transcription factors with serum response factor: identification of the Elk-1 binding surface.

Ling, Y., West, A.G., Roberts, E.C., Lakey, J.H., and Sharrocks, A.D. (1998) Interaction of transcription factors with serum response factor: identification of the Elk-1 binding surface. Journal of Biological Chemistry, 273 (17). pp. 10506-10514. ISSN 0021-9258

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Abstract

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.

Item Type:Article
Status:Published
Refereed:Yes
Glasgow Author(s):West, Dr Adam
Authors: Ling, Y., West, A.G., Roberts, E.C., Lakey, J.H., and Sharrocks, A.D.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
Journal Name:Journal of Biological Chemistry
Journal Abbr.:J Biol Chem.
Publisher:American Society for Biochemistry and Molecular Biology, Inc.
ISSN:0021-9258
ISSN (Online):1083-351X
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