Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
52
pubmed:dateCreated
2001-12-25
pubmed:abstractText
We have used a combination of fluorescence anisotropy spectroscopy and fluorescence-based native gel electrophoresis methods to examine the effects of the transcription factor IID-specific subunit TAF130p (TAF145p) upon the TATA box DNA binding properties of TATA box-binding protein (TBP). Purified full-length recombinant TAF130p decreases TBP-TATA DNA complex formation at equilibrium by competing directly with DNA for binding to TBP. Interestingly, we have found that full-length TAF130p is capable of binding multiple molecules of TBP with nanomolar binding affinity. The biological implications of these findings are discussed.
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/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TAF1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated..., http://linkedlifedata.com/resource/pubmed/chemical/TATA-Box Binding Protein, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49100-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11677244-DNA, pubmed-meshheading:11677244-DNA-Binding Proteins, pubmed-meshheading:11677244-Electrophoresis, pubmed-meshheading:11677244-Fluorescence Polarization, pubmed-meshheading:11677244-Macromolecular Substances, pubmed-meshheading:11677244-Protein Binding, pubmed-meshheading:11677244-Protein Subunits, pubmed-meshheading:11677244-Recombinant Proteins, pubmed-meshheading:11677244-Saccharomyces cerevisiae, pubmed-meshheading:11677244-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11677244-Spectrometry, Fluorescence, pubmed-meshheading:11677244-TATA Box, pubmed-meshheading:11677244-TATA-Binding Protein Associated Factors, pubmed-meshheading:11677244-TATA-Box Binding Protein, pubmed-meshheading:11677244-Transcription Factor TFIID, pubmed-meshheading:11677244-Transcription Factors
pubmed:year
2001
pubmed:articleTitle
Fluorescence-based analyses of the effects of full-length recombinant TAF130p on the interaction of TATA box-binding protein with TATA box DNA.
pubmed:affiliation
Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232-0615, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.