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Volume 271, Number 39, Issue of September 27, 1996 pp. 23999-24004
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Effect of DNA-binding Drugs on Early Growth Response Factor-1 and TATA Box-binding Protein Complex Formation with the Herpes Simplex Virus Latency Promoter

(Received for publication, April 17, 1996, and in revised form, July 9, 1996)

Shu-Yuan Chiang , John J. Welch , Frank J. Rauscher III^§ and Terry A. Beerman

From the  Experimental Therapeutics Department, Roswell Park Cancer Institute, Buffalo, New York 14263 and ^§ The Wistar Institute, Philadelphia, Pennsylvania 19104

Adjacent binding sites for early growth response factor-1 (EGR1) and TATA box-binding protein (TBP) were identified on the herpes simplex virus latency promoter in previous work. The binding of EGR1 to the GC-rich region prevented TBP binding to the AT-rich region. With the simultaneous addition of both EGR1 and TBP, the intercalator nogalamycin prevented EGR1 complex formation, resulting in a dose-dependent increase of the TBP·DNA complex. The minor groove binder chromomycin A₃ inhibited EGR1 complex formation but resulted in a smaller increase of the TBP complex. In contrast, an alkylating intercalator hedamycin strongly inhibited binding of both proteins. The ability of these GC-binding drugs to prevent EGR1·DNA complex formation was in the following order: hedamycin > nogalamycin > chromomycin A₃, and the specificity was nogalamycin > chromomycin A₃ > hedamycin. With transcription factor IIA (TFIIA) in the assay, TBP was able to bind the promoter whereas formation of the EGR1·DNA complex was reduced. An AT minor groove-binding drug, distamycin A, disrupted the TBP·TFIIA·DNA complex and restored the EGR1·DNA complex. We conclude that the binding motif and sequence preference of DNA-interactive drugs are manifested in their ability to inhibit the transcription factor-DNA complexes.

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