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Nucleic Acids Research, 1990, Vol. 18, No. 8 1991-1999
© 1990

MOLECULAR BIOLOGY

Macromolecular interaction on a cAMP responsive region in the urokinase-type plasminogen activator gene: a role of protein phosphorylation

Dietmar von der Ahe1,*, David Pearson2,* and Yoshikuni Nagamine+

Friedrich Miescher-Institut CH-4002 Basel, Switzerland

+ To whom correspondence should be addressed at Friedrich Miescher-Institut, Postfach 2543, CH-4002 Basel, Switzerland

Received January 23, 1990. Revised March 20, 1990. Accepted March 20, 1990.

We have studied the regulation of urokinase-type plasminogen activator gene expression by cAMP in LLC-PK1 cells. We found a cAMP responsive region 3.4 kb upstream of the transcription initiation site, which comprised three protein-binding domains designated A, B, and C. Domains A and B both contain a sequence, TGACG, homologous to a consensus cAMP response element (CRE; TGACGTCA). Effective cAMP-mediated induction was achieved when these two domains were linked with domain C, which by itself did not confer cAMP responsiveness to a heterologous promoter nor contained CRE-like sequence, suggesting a functional cooperation among these domains. Results of competition studies using gel retardation and DNase I footprinting assays suggest that there is a protein-protein interaction between a CRE binding protein and a domain C binding protein. In gel retardation assays, binding of a nuclear protein to domains A and B was strongly augmented by addition of the catalytic subunit of cAMP-dependent protein kinase, whereas the protein binding to domain C was slightly inhibited, suggesting that protein phosphorylation is involved in the regulation of protein-DNA interaction.

1Present addresses: Max-Planck Clinical Research Group for Blood Coagulation and Thrombosis, Gaffkystrasse 11, D-6300 Giessen, FRG

2Present addresses: Shriners Hospital for Crippled Children, 12505 North Pine Drive, Tampa, FL 33612-9499, USA

*D. v.d.A and D. P contributed equally to the work


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