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J Biol Chem, Vol. 273, Issue 22, 13387-13390, May 29, 1998
,,
From the Department of Biochemistry, Case Western Reserve
University School of Medicine, Cleveland, Ohio 44106-4935, the
Nuclear factor-I (NFI) binds to the
phosphoenolpyruvate carboxykinase (GTP) (PEPCK) gene promoter
immediately 5' to the cAMP regulatory element (CRE). This suggests an
interaction between NFI and factors that bind the CRE. Of the four NFI
isoforms expressed in mammalian tissues, NFI-A and -B stimulate basal
transcription from the PEPCK gene promoter in HepG2 cells, while NFI-C
and -X are slightly inhibitory. All four NFI isoforms abrogate the
20-fold protein kinase Ac (PKAc)-mediated induction of transcription
from the PEPCK gene promoter. Normal PKAc-mediated induction was noted when the CRE was moved 10 base pairs 3' of its original location. However if the CRE was moved 5 base pairs 3', placing it out of phase
with the other elements in the promoter, or moved 5' to Department of Cancer Biology, Lerner Research Institute,
Cleveland Clinic Foundation, Cleveland, Ohio 44106, and the
** Department of Biochemistry, University of Saskatchewan,
Saskatoon, Saskatchewan S7N 5E5, Canada
285 (the
P3(I) site in the promoter), some PKA-mediated stimulation was lost.
The NFI-C isoform effectively inhibited PKAc induction regardless of
the relative positions of the CRE and the NFI binding sites. NFI-C also
abrogated cAMP regulatory element-binding protein (CREB)-induced
activity of wild type and mutant PEPCK promoters. There was some
cooperativity in the binding of CREB and NFI to their respective
binding sites but this did not appear to be physiologically important.
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