Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-7-12
pubmed:abstractText
Specific interactions between DNA and transcription factors are necessary for transcription initiation. These interactions provide a potential target for the selective inhibition of eukaryotic gene expression. Mithramycin is a DNA binding antibiotic which, in the presence of Mg2+, binds G-C containing sequences in the minor groove. The SV40 early promoter contains six G-C decanucleotide sequences, which are binding sites for the transcriptional activating factor, Sp1. Each of the six Sp1 binding sites of this promoter is protected from DNAse 1 digestion by mithramycin binding. Mithramycin binding to the G-C rich sequences in the SV40 early promoter prevents subsequent protein binding to these sequences. The gel retardation of the SV40 early promoter fragment incubated with a HeLa cell extract is completely abrogated by pretreatment of the DNA fragment with mithramycin. The functional significance of mithramycin binding is reflected in the ability of mithramycin to block promoter function. Mithramycin inhibits promoter dependent transcription in an in vitro runoff transcription system in a concentration dependent manner. This suggests that mithramycin prevents transcriptional activation of the SV40 early promoter by blocking binding of transcriptional activating proteins to G-C rich promoter regions.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2421408, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2431313, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2444981, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2943018, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2962490, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2991898, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2992804, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-2993923, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3012774, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3024847, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3027570, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3096580, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3160729, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3280975, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3319186, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3461465, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3529394, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-3945313, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-4041012, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-5901746, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6187469, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6204275, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6222762, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6246368, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6300662, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6313230, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6356356, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6722879, http://linkedlifedata.com/resource/pubmed/commentcorrection/2542379-6828386
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9738
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2003-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Mithramycin blocks protein binding and function of the SV40 early promoter.
pubmed:affiliation
Department of Internal Medicine and Biochemistry, University of Alabama, Birmingham 35294.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't