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Nucleic Acids Research, 1991, Vol. 19, No. 12 3369-3375
© 1991

MOLECULAR BIOLOGY

Mammalian ß-polymerase promoter: phosphorylation of ATF/CRE-binding protein and regulation of DNA binding

Ella W. Englander, Steven G. Widen and Samuel H. Wilson

Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health Bethesda, MD 20892, USA

Received February 20, 1991. Revised May 6, 1991. Accepted May 6, 1991.

The gene for the mammalian DNA repair enzyme DNA polymerase ß (fiß-pol) is constitutively expressed in most cells, but is regulated in a tissue-specific fashion and can be induced in response to some types of DNA damaging agents. The promoter for the human ß-pol gene has been characterized and found to be TATA-less, but it does have multiple GC boxes and one ATF/CRE-bindlng site located within 50 residues 5' of the major mRNA start site. The ATF/CRE-bindlng site has been found to be essential for activity of the cloned promoter. We report that a bovine testes DNA-binding protein with specificity for the ß-pol promoter ATF/CRE-binding site is phosphorylated in vivo and contains several phosphorylation sites. Sequence specific DNA-binding by the purified protein is reduced when the natural protein is dephosphorylated or when it is hyperphosphorylated by protein kinase A (cKA) in vitro. These results suggest the possibility that phosphorylation systems may change binding of this ATF/CRE-blnding protein to the ß-pol promoter and in turn modulate the promoter. Possible correlation of the results with transient expression activity of the cloned ß-pol promoter fusion gene was obtained in 293 cells. Cotransfection with a cKA expression plasmid to elevate phosphorylation was found to strongly reduce promoter activity.


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