Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1991-7-24
pubmed:abstractText
We recently reported that the apparently non-DNA-binding 65 kd subunit (p65) of the NF-kappa B transcription factor can modulate the DNA-binding specificity of the 50 kd subunit (p50) of NF-kappa B. In this study we provide an explanation for this property of p65. In electrophoretic mobility shift assays and upon UV cross-linking to DNA, gel-purified p65 is shown to be a kappa B-specific DNA-binding protein on its own. The binding activity was only detectable if high amounts of p65 were used for the analyses and after the application of a modified renaturation protocol. DNA-binding of the p65 dimer, in contrast to that of p50, was inhibited by I kappa B-alpha and -beta. This finding is consistent with a receptor function of p65 for both inhibitory subunits. Direct UV cross-linking of NF-kappa B to DNA probes which were photoreactive within only one half-site and a binding competition analysis with p65 showed that p65 has a strong preference for binding to the less conserved half site of kappa B motifs whereas p50 has a moderate preference for the more highly conserved half site. In electrophoretic mobility shift assays and upon sedimentation through glycerol gradients, NF-kappa B appears to exist as a heterodimer composed of one p50 and one p65 subunit whereas data from gel filtration suggest a higher order complex.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-1985897, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2006423, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2106065, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2125960, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2157987, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2174540, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2181276, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2184941, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2203531, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2203532, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2225078, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2234062, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2494701, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2494702, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2495183, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2663471, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-2691328, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-3133660, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-3140380, http://linkedlifedata.com/resource/pubmed/commentcorrection/2050119-3678204
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1817-25
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
NF-kappa B contacts DNA by a heterodimer of the p50 and p65 subunit.
pubmed:affiliation
Laboratorium für Molekulare Biologie, Ludwig-Maximilians-Universität München, Martinsried, FRG.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't