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Nucleic Acids Research, 1987, Vol. 15, No. 24 10145-10158
© 1987

Articles

Purification of intercalator-released p67, a polypeptide that interacts specifically with the c-fos serum response element

Hennrick Schröter, Peter E. Shaw and Alfred Nordheim

Zentrum fur Molekulare Biologie (ZMBH), Universitat Heidelberg Im Neuenheimer Feld 282, D-6900 Heidelberg, FRG

Received October 16, 1987. Accepted November 27, 1987.

Incubation of intact nuclei in buffers containing the DNA intercalating drug chloroquine leads to release of proteins that interact with DNA (1). We demonstrate here that a protein which binds to a motif within the human c-fos promoter, identified as the serum response element (SRE), is quantitatively released from HeLa nuclei, whereas nuclear factor 1 (NF 1) is not. Purification of the SRE binding protein by affinity chromatography to greater than 95% homogeneity allowed us to identify it as a polypeptide of approximately 67,000 daltons. The DNA contacts made by p67, as identified by methylation interference experiments, are indistinguishable from those of the serum response factor described previously (2).


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