Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1993-7-27
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14497-504
pubmed:dateRevised
2008-11-21
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
pubmed:year
1993
pubmed:articleTitle
Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization.
pubmed:affiliation
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't