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Nucleic Acids Research, 1993, Vol. 21, No. 8 1845-1852
© 1993

MOLECULAR BIOLOGY

Purification and cDNA cloning of a transcription factor which functionally cooperates within a cAMP regulatory unit in the porcine uPA gene

Pierre-Alain Menoud, Renate Matthies, Jan Hofsteenge and Yoshikuni Nagamine*

Friedrich Miescher-lnstitut Postfach 2543, CH-4002 Basel, Switzerland

*To whom correspondence should be addressed

Received January 5, 1993. Revised March 16, 1993. Accepted March 16, 1993.

One of cAMP-regulatory sites In the porcine uroklnase-type plasmlnogen activator (uPA) gene resides 3.4 kb upstream of the transcription Initiation site and Is composed of three protein binding domains, FPA, FPB and FPC. Whereas FPA and FPB contain a CRE-IIke sequence, the FPC sequence Is not related to any known protein recognition sequences, yet all three domains are required to mediate cAMP action on a heterologous promoter. To study the functional cooperation among these three domains we purified and cloned a FPC-blndlng protein (FPCB) from porcine kidney derived LLC-PIC, cells. Sequence comparisons showed that FPCB Is homologous to mouse LFB3 and rat vHNFL LFB3/vHNF1 is related to a liver specific transcription factor HNF1, It recognizes the same sequence as HNF1 and is highly expressed In kidney cells. FPCB and HNF1 recognition sequences are dissimilar, nevertheless both sequences are recognized by in vitro-translated LFB3 and FPCB, Indicating that binding to the two different sequences is an intrinsic character of FPCB/LFB3/vHNF1. In HeLa cells, this cAMP-responsive site was inactive whether FPCB was overexpressed or not, suggesting a requirement for an additional cell-specific factor. These results may suggest a mechanism by which hormonal control is integrated Into cell-specific gene regulation.


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