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Nucleic Acids Research, 2000, Vol. 28, No. 2 560-569
© 2000 Oxford University Press

The mechanism of complex formation between Fli-1 and SRF transcription factors

Pamela Dalgleish and Andrew D. Sharrocks*

Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, UK

The mechanisms of multicomponent transcription factor complex assembly are currently poorly defined. A paradigm for this type of complex is the ETS-domain transcription factor Elk-1 and the MADS-box transcription factor SRF which form a ternary complex with the c-fos serum response element (SRE). In this study we have analysed how a different ETS-domain transcription factor Fli-1 interacts with SRF to form ternary complexes with this element. Two regions of Fli-1 that are required for ternary complex formation have been identified. These SRF binding motifs are located on either side of the ETS DNA-binding domain. Hydrophobic amino acids within these motifs have been identified that play important roles in binding to SRF and ternary complex formation. By using Fli-1 derivatives with mutations in the N-terminal SRF binding motif, the significance of Fli-1–SRF interactions in recruitment of Fli-1 to the c-fos SRE in vivo has been demonstrated. Collectively our data provide a model of how Fli-1 interacts with SRF that differs significantly from the mechanism used by a different ETS-domain protein, Elk-1.

* To whom correspondence should be addressed at present address: School of Biological Sciences, Stopford Building, University of Manchester, Oxford Road, Manchester M13 9PT, UK. Tel: +44 161 275 5979; Fax: +44 161 275 5082; Email: a.d.sharrocks@man.ac.uk


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