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J Biol Chem, Vol. 273, Issue 8, 4585-4591, February 20, 1998
From the Laboratory of Molecular Endocrinology, CHUL Research
Centre and Laval University, Sainte-Foy,
Québec, G1V 4G2, Canada
Regulation of the human CYP11A gene
encoding cytochrome P450scc, which catalyzes the first step of steroid
synthesis, is regulated by many trans-acting transcription
factors including steroidogenic factor 1 (SF-1). Transfection
experiments in human adrenal NCI-H295 cells demonstrate
regulation of the P450scc gene promoter region that contains several
putative SF-1 binding sites. Cotransfection of SF-1 with a
luciferase reporter construct containing the P450scc gene 5'-flanking
region from nucleotides
Regulation of the Human P450scc Gene by Steroidogenic Factor
1 Is Mediated by CBP/p300
1676 to +49 increased promoter activity, and
deletion of the nucleotide sequence from position 1676 to 1620,
which removes a putative cAMP response element (CRE), did not affect
the stimulatory response to SF-1. As well, further deletion of the
promoter region to nucleotide 110, which contains only one SF-1
binding site, still retained the ability to respond to exogenous SF-1.
However, mutation of the remaining site which abolished SF-1
protein/DNA interaction also abrogated any functional response to the
factor. All the P450scc reporter constructs which responded to SF-1
were further stimulated by exogenous p300 and CREB-binding protein
(CBP), suggesting interaction between SF-1 and p300/CBP. As well,
mutation of the binding site that abrogated the response to SF-1 also
abolished the response to p300 and CBP. Cotransfection of the
adenovirus E1A oncoprotein, which has been shown to interact with
p300/CBP and interfere with its function, decreased the stimulatory
effect of SF-1 and p300/CBP. Cotransfection of a mutated E1A protein, RG2, which does not interact with p300/CBP, did not alter the stimulatory effect of SF-1 and p300/CBP on the P450scc promoter. Deletion of the region from amino acid residues 2-67 in E1A, which has
been postulated to interact with p300/CBP, also abolished the
inhibitory effect of E1A, whereas deletion of the region from residues
120 to 140 had no effect. Two regions of CBP from amino acids 1 to 451 and from 1460 to 1891 were demonstrated to interact with SF-1 in
vitro. Coexpression of fragments of the p300 protein fused to the
VP16 protein in the presence of SF-1 and the 110 P450scc reporter
construct indicated in vivo the interaction of two regions
of p300 with SF-1, thus confirming the in vitro results. Taken together these results indicate that regulation of the human P450scc gene by SF-1 is mediated by p300/CBP. Due to the many putative
roles of SF-1 to regulate many genes, its interaction with p300/CBP is
potentially a key component effecting important physiological
processes.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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H. Pincas, J.-N. Laverriere, and R. Counis |
