Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
1995-9-18
pubmed:abstractText
The ubiquitous human POU domain protein, Oct-1, and the related B-cell protein, Oct-2, regulate transcription from a variety of eukaryotic genes by binding to a common cis-acting octamer element, 5'-ATTTGCAT-3'. The binding of Oct-1 and Oct-2 to the functionally important lipoprotein lipase (LPL) promoter octamer site was stimulated by the general transcription factor, TFIIB. Comparative analysis of the LPL, histone H2B (H2B), and herpes simplex virus ICPO gene promoter octamer sites revealed that nucleotide sequences within and flanking the octamer sequence determined the degree of TFIIB-mediated stimulation of Oct-1 DNA binding. TFIIB was found to decrease the rate of dissociation of Oct-1 from the LPL octamer site, whereas it increased the rate of association, as well as decreased the rate of dissociation, of Oct-1 from the H2B octamer site. A monoclonal antibody against TFIIB immunoprecipitated a ternary complex containing TFIIB, Oct-1, and the LPL and H2B octamer binding sites. TFIIB did not alter the DNase I footprints generated by Oct-1 on the LPL and H2B promoters. However, Oct-1 on the TATA-binding protein and TFIIB from footprinting the perfect TATA box sequence located 5' of the LPL, NF-Y binding site. In transfection experiments, transcription from the reporters containing the LPL octamer, and either the SV40 or the yeast transcription factor GAL4-dependent enhancers, initiated at a precise position within the octamer sequence. Transcription from reporters containing the H2B octamer and the SV40 enhancer initiated at several positions within and flanking the octamer site, whereas transcription initiated at a precise position within the octamer from reporters with both the H2B octamer and the GAL4-dependent enhancer. These results suggest that octamers and their flanking sequences play an important role in positioning the site of transcription initiation, and that this could be a function of the interaction of Oct-1 with TFIIB.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I, http://linkedlifedata.com/resource/pubmed/chemical/Hcfc1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Host Cell Factor C1, http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase, http://linkedlifedata.com/resource/pubmed/chemical/Octamer Transcription Factor-1, http://linkedlifedata.com/resource/pubmed/chemical/Octamer Transcription Factor-2, http://linkedlifedata.com/resource/pubmed/chemical/Pou2f1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Pou2f2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIB, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19613-23
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7642649-3T3 Cells, pubmed-meshheading:7642649-Animals, pubmed-meshheading:7642649-Base Sequence, pubmed-meshheading:7642649-DNA, pubmed-meshheading:7642649-DNA-Binding Proteins, pubmed-meshheading:7642649-Deoxyribonuclease I, pubmed-meshheading:7642649-Host Cell Factor C1, pubmed-meshheading:7642649-Lipoprotein Lipase, pubmed-meshheading:7642649-Mice, pubmed-meshheading:7642649-Molecular Sequence Data, pubmed-meshheading:7642649-Octamer Transcription Factor-1, pubmed-meshheading:7642649-Octamer Transcription Factor-2, pubmed-meshheading:7642649-Promoter Regions, Genetic, pubmed-meshheading:7642649-Protein Binding, pubmed-meshheading:7642649-Recombinant Proteins, pubmed-meshheading:7642649-Sequence Deletion, pubmed-meshheading:7642649-TATA Box, pubmed-meshheading:7642649-Transcription Factor TFIIB, pubmed-meshheading:7642649-Transcription Factors
pubmed:year
1995
pubmed:articleTitle
Interaction of Oct-1 with TFIIB. Implications for a novel response elicited through the proximal octamer site of the lipoprotein lipase promoter.
pubmed:affiliation
Laboratory of Gene Regulation, Picower Institute for Medical Research, Manhasset, New York 11030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't