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rdf:type |
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lifeskim:mentions |
umls-concept:C0013227,
umls-concept:C0018270,
umls-concept:C0086860,
umls-concept:C0144555,
umls-concept:C0206188,
umls-concept:C0206558,
umls-concept:C0871261,
umls-concept:C1158923,
umls-concept:C1280500,
umls-concept:C1337106,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
39
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pubmed:dateCreated |
1996-11-18
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pubmed:abstractText |
Adjacent binding sites for early growth response factor-1 (EGR1) and TATA box-binding protein (TBP) were identified on the herpes simplex virus latency promoter in previous work. The binding of EGR1 to the GC-rich region prevented TBP binding to the AT-rich region. With the simultaneous addition of both EGR1 and TBP, the intercalator nogalamycin prevented EGR1 complex formation, resulting in a dose-dependent increase of the TBP.DNA complex. The minor groove binder chromomycin A3 inhibited EGR1 complex formation but resulted in a smaller increase of the TBP complex. In contrast, an alkylating intercalator hedamycin strongly inhibited binding of both proteins. The ability of these GC-binding drugs to prevent EGR1.DNA complex formation was in the following order: hedamycin > nogalamycin > chromomycin A3, and the specificity was nogalamycin > chromomycin A3 > hedamycin. With transcription factor IIA (TFIIA) in the assay, TBP was able to bind the promoter whereas formation of the EGR1.DNA complex was reduced. An AT minor groove-binding drug, distamycin A, disrupted the TBP.TFIIA.DNA complex and restored the EGR1.DNA complex. We conclude that the binding motif and sequence preference of DNA-interactive drugs are manifested in their ability to inhibit the transcription factor-DNA complexes.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkylating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Anthraquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Chromomycin A3,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Distamycins,
http://linkedlifedata.com/resource/pubmed/chemical/EGR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Early Growth Response Protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intercalating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Nogalamycin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TATA-Box Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIA,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/hedamycin,
http://linkedlifedata.com/resource/pubmed/chemical/stallimycin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23999-4004
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8798634-Alkylating Agents,
pubmed-meshheading:8798634-Anthraquinones,
pubmed-meshheading:8798634-Base Composition,
pubmed-meshheading:8798634-Chromomycin A3,
pubmed-meshheading:8798634-DNA-Binding Proteins,
pubmed-meshheading:8798634-Deoxyribonucleoproteins,
pubmed-meshheading:8798634-Distamycins,
pubmed-meshheading:8798634-Early Growth Response Protein 1,
pubmed-meshheading:8798634-Gene Expression Regulation, Viral,
pubmed-meshheading:8798634-Humans,
pubmed-meshheading:8798634-Immediate-Early Proteins,
pubmed-meshheading:8798634-Intercalating Agents,
pubmed-meshheading:8798634-Macromolecular Substances,
pubmed-meshheading:8798634-Nogalamycin,
pubmed-meshheading:8798634-Promoter Regions, Genetic,
pubmed-meshheading:8798634-Recombinant Fusion Proteins,
pubmed-meshheading:8798634-Simplexvirus,
pubmed-meshheading:8798634-TATA-Box Binding Protein,
pubmed-meshheading:8798634-Transcription Factor TFIIA,
pubmed-meshheading:8798634-Transcription Factors,
pubmed-meshheading:8798634-Virus Latency
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pubmed:year |
1996
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pubmed:articleTitle |
Effect of DNA-binding drugs on early growth response factor-1 and TATA box-binding protein complex formation with the herpes simplex virus latency promoter.
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pubmed:affiliation |
Experimental Therapeutics Department, Roswell Park Cancer Institute, Buffalo, New York 14263, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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