NDLI: Sterol regulatory element binding protein binds to a cis element in the promoter of the farnesyl diphosphate synthase gene.

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Sterol regulatory element binding protein binds to a cis element in the promoter of the farnesyl diphosphate synthase gene.

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Sterol regulatory element binding protein binds to a cis element in the promoter of the farnesyl diphosphate synthase gene.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ericsson, J. Edwards, P. A. Jackson, S. M. Lee, B. C.
Description	Author Affiliation: Ericsson J ( Department of Biological Chemistry, University of California, Los Angeles 90095, USA.);
Abstract	Sterol-regulated transcription of the gene for rat farnesyl diphosphate (FPP) synthase (geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase, EC 2.5.1.10) is dependent in part on the binding of the ubiquitous transcription factor NF-Y to a 6-bp element within the proximal promoter. Current studies identify a second element in this promoter that is also required for sterol-regulated transcription in vivo. Mutation of three nucleotides (CAC) within this element blocks the 8-fold induction of FPP synthase promoter-reporter genes that normally occurs when the transfected cells are incubated in medium deprived of sterols. Gel mobility-shift assays demonstrate that the transcriptionally active 68-kDa fragment of the sterol regulatory element (SRE-1)-binding protein assays (SREBP-1) binds to an oligonucleotide containing the wild-type sequence but not to an oligonucleotide in which the CAC has been mutated. DNase 1 protection pattern (footprint) analysis indicates that SREBP-1 binds to nucleotides that include the CAC. Both the in vivo and in vitro assays are affected by mutagenesis of nucleotides adjacent to the CAC. Coexpression of SREBP with a wild-type FPP synthase promoter-reporter gene in CV-1 cells results in very high levels of reporter activity that is sterol-independent. In contrast, the reporter activity remained low when the promoter contained a mutation in the CAC trinucleotide. We conclude that sterol-regulated transcription of FPP synthase is controlled in part by the interaction of SREBP with a binding site that we have termed SRE-3. Identification of this element may prove useful in the identification of other genes that are both regulated by SREBP and involved in lipid biosynthesis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alkyl And Aryl Transferases CCAAT-Enhancer-Binding Proteins DNA-Binding Proteins Metabolism Gene Expression Regulation, Enzymologic Nuclear Proteins Promoter Regions, Genetic Transcription Factors Transferases Genetics Animals Binding Sites Cells, Cultured DNA Footprinting Genes, Reporter Geranyltranstransferase Molecular Sequence Data Mutagenesis Protein Binding Sterol Regulatory Element Binding Protein 1 Transfection Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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