Nucleic Acids Research, 1995, Vol. 23, No. 13 2442-2449
© 1995
MOLECULAR BIOLOGY |
DNA bending in the ternary nucleoprotein complex at the c-fos prometer
Department of Biochemistry and Genetics, The Medical School University of Newscastle Upon Tyne Newcastle Upon Tyne, UK
*To whom corespondence should be addressed
Received April 3, 1995. Accepted May 19, 1995.
Transcriptional induction of the c-fos protc-oncogene in response to serum growth factors is mediated in part by a ternary complex that forms on the serum response element (SRE) within Its promoter. This complex consists of Elk-1, serum response factor (SRF) and the SRE. Elk-1 Is phosphorylated by MAP kinase, which correlates with the induction of c-fos transcription. In this study we have investigated the protein-induced DNA bending which occurs during the formation and post-translational modification of the ternary complex that forms at the c-fos SRE. Circular permutation analysis demonstrates that the minimal DNA-blnding domain of SRF, which contains the MADS box, is sufficient to Induce flexibility into the centre of its binding site within the SRE. Phasing analysis indicates that at least part of this flexibility results in the production of a directional bend towards the minor groove. The Isolated ETS domains from Elk-1 and SAP-1 induce neither DNA bending nor increased DNA flexibility. Formation of ternary complexes by binding of Elk-1 to the binary SRF:SRE complex results In a change in the flexibility of the SRE. Phosphorylatlon of Elk-1 by MAP kinase (p42/ERK2) induces urther minor changes In this DNA flexiility. However, phasinganalysis reveals that the recruitment of Elk-1 to form the ternary complex affects the SRF-induced directional DNA bend in the SRE. The potetial roles of DNA bending at the c-fos SR are discussed.
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