rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1993-7-27
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pubmed:abstractText |
This paper describes the purification and characterization of a sterol regulatory element binding protein (SREBP) that recognizes the SRE-1 sequence in the 5' flanking region of the gene for the low density lipoprotein (LDL) receptor. The protein was purified more than 38,000-fold from nuclear extracts of human HeLa cells by ion exchange, gel filtration, and DNA-affinity chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified preparation revealed a cluster of bands at 59-68 kDa, each of which bound to the SRE-1 element as revealed by cross-linking experiments. Binding of SREBP correlated perfectly with transcriptional activity in a series of 16 sterol regulatory elements with point mutations. In the LDL receptor promoter, the 10-base pair SRE-1 is embedded in a 16-base pair sequence designated Repeat 2, which is adjacent to Repeat 3, a binding site for nuclear factor Sp1. Oligonucleotides containing Repeat 2 + 3 bound SREBP and Sp1 as revealed by mobility shift assays. SREBP produced a DNase I footprint over the SRE-1 sequence, which was immediately adjacent to the footprint produced by Sp1. The current data are consistent with the concept that SREBP acts in concert with Sp1 to achieve high level, sterol-suppressible transcription of the gene for the LDL receptor.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCAAT-Enhancer-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/SREBF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol Regulatory Element Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Sterols,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14497-504
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8314806-Base Sequence,
pubmed-meshheading:8314806-Binding Sites,
pubmed-meshheading:8314806-CCAAT-Enhancer-Binding Proteins,
pubmed-meshheading:8314806-Cell Nucleus,
pubmed-meshheading:8314806-Chromatography, Affinity,
pubmed-meshheading:8314806-Chromatography, Gel,
pubmed-meshheading:8314806-Chromatography, Ion Exchange,
pubmed-meshheading:8314806-DNA-Binding Proteins,
pubmed-meshheading:8314806-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8314806-HeLa Cells,
pubmed-meshheading:8314806-Humans,
pubmed-meshheading:8314806-Kinetics,
pubmed-meshheading:8314806-Molecular Sequence Data,
pubmed-meshheading:8314806-Molecular Weight,
pubmed-meshheading:8314806-Nuclear Proteins,
pubmed-meshheading:8314806-Oligodeoxyribonucleotides,
pubmed-meshheading:8314806-Point Mutation,
pubmed-meshheading:8314806-Promoter Regions, Genetic,
pubmed-meshheading:8314806-Receptors, LDL,
pubmed-meshheading:8314806-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:8314806-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8314806-Sterol Regulatory Element Binding Protein 1,
pubmed-meshheading:8314806-Sterols,
pubmed-meshheading:8314806-Substrate Specificity,
pubmed-meshheading:8314806-Transcription Factors
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pubmed:year |
1993
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pubmed:articleTitle |
Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization.
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pubmed:affiliation |
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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