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J Biol Chem, Vol. 275, Issue 17, 12497-12502, April 28, 2000
From the In an attempt to identify unknown target genes
for SREBP-1, total RNA from a stable Chinese hamster ovary cell line
(CHO-487) expressing a mature form of human SREBP-1a (amino acids
1-487) with a LacSwitch Inducible Mammalian Expression System was
subjected to a polymerase chain reaction subtraction method. One of the fragments was found to have 90 and 86% homology with rat and human ATP
citrate-lyase (ACL) cDNA, respectively. When Hep G2 cells are
cultured under either sterol-loaded or -depleted conditions, expression
of the gene is induced approximately 2-3-fold by sterol depletion. To
investigate the direct effect of SREBP-1a on transcription, luciferase
assays using the promoter of the human ACL gene were performed. These
deletion studies indicated that a minimum 160-base pair segment
contains the information required for the transcriptional regulation
brought about by enforced expression of SREBP-1a. Luciferase assays
using mutant reporter genes revealed that SREBP-dependent transcriptional regulation is mediated by two nearby motifs, the SREBP-binding site (a TCAGGCTAG sequence) and the NF-Y-binding site (a
CCAAT box). It was confirmed by gel mobility shift assays that
recombint SREBP-1a binds to the sequence. Data from studies with
transgenic mice and reporter assays show that the ACL gene promoter is
activated by SREBP-1a more strongly than SREBP-2 in contrast to the HMG
CoA synthase and LDL receptor gene promoters, which exhibit the same
preference for the two factors. Therefore, SREBPs transcriptionally
regulates ACL enzyme activity, which generates the cytosolic acetyl CoA
required for both cholesterol and fatty acid synthesis.
Transcriptional Regulation of the ATP Citrate-lyase Gene by
Sterol Regulatory Element-binding Proteins*
§¶,
, Department of Applied Biological Chemistry,
Graduate School of Agricultural and Life Sciences, The University of
Tokyo, Tokyo 113-8657, § Laboratory of Biochemistry and
Molecular Biology, Graduate School of Pharmaceutical Sciences, Osaka
University, Osaka 565-0871, the International Center for Medical
Research, Kobe University School of Medicine, Kobe 650-0017, and the
** Department of Metabolic Diseases, Faculty of Medicine, The University
of Tokyo, Tokyo 113-8655, Japan
*
This work was supported by grants from the Ministry of
Education, Scinece, Sports, and Culture of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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