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Nucleic Acids Research, 1989, Vol. 17, No. 22 9291-9304
© 1989

MOLECULAR BIOLOGY

Functional analysis of GC element binding and transcription in the hamster dihydrofolate reductase gene promoter

Andrew G. Swick1, Michael C. Blake1,3, Jeanne W. Kahn1 and Jane Clifford Azizkhan1,2,3,*

1Lineberger Cancer Research Center, University of North Carolina Chapel Hill, NC 27599-7295, USA 2Department of Pediatrics and Pharmacology, University of North Carolina Chapel Hill, NC 27599-7295, USA 3Curriculum in Genetics, University of North Carolina Chapel Hill, NC 27599-7295, USA

*To whom correspondence should be addressed

Received July 13, 1989. Revised October 4, 1989. Accepted October 4, 1989.

Dihydrofolate reductase (DHFR) gene expression is required for cell growth. The DHFR gene promoter contains several GC elements capable of binding the transcription factor Sp1 In this report we have characterized the effect of protein(s) binding to these sequence elements in the Chinese hamster DHFR promoter on transcription. We have constructed a series of deletions containing from 896 to 103 bp 5' to the start of translation. The protein binding domains have been mapped by DNAse I footprint analysis using HeLa nuclear extract, and the function of the protein-binding elements has been assessed by in vitro transcription and transient CAT expression. Maximal transcription in vitro and CAT expression is obtained with a construct containing 3 GC elements extending to position -184. Removal of GC element binding factor(s), by competition with an oligonucleotide containing an Sp1 binding site, completely abolishes transcription in vitro and significantly diminishes CAT expression. Ten-fold higher molar excess of competitor is required to abolish SV40 early transcription, suggesting that the GC element interactions in the DHFR promoter are different from those in the SV40 early region. Co-transfection of a DHFR CAT construct with an expressor of Sp1 dramatically increased CAT expression in Drosophila cells.


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