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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
38
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pubmed:dateCreated |
1991-10-23
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pubmed:abstractText |
A class of triplex-forming oligodeoxyribonucleotides (TFOs) is described that can bind to naturally occurring sites in duplex DNA at physiological pH in the presence of magnesium. The data are consistent with a structure in which the TFO binds in the major groove of double-stranded DNA to form a three-stranded complex that is superficially similar to previously described triplexes. The distinguishing features of this class of triplex are that TFO binding apparently involves the formation of hydrogen-bonded G.GC and T.AT triplets and the TFO is bound antiparallel with respect to the more purine-rich strand of the underlying duplex. Triplex formation is described for targets in the promoter regions of three different genes: the human c-myc and epidermal growth factor receptor genes and the mouse insulin receptor gene. All three sites are relatively GC rich and have a high percentage of purine residues on one strand. DNase I footprinting shows that individual TFOs bind selectively to their target sites at pH 7.4-7.8 in the presence of millimolar concentrations of magnesium. Electrophoretic analysis of triplex formation indicates that specific TFOs bind to their target sites with apparent dissociation constants in the 10(-7)-10(-9) M range. Strand orientation of the bound TFOs was confirmed by attaching eosin or an iron-chelating group to one end of the TFO and monitoring the pattern of damage to the bound duplex DNA. Possible hydrogen-bonding patterns and triplex structures are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9246-55
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1892832-Animals,
pubmed-meshheading:1892832-Base Sequence,
pubmed-meshheading:1892832-Deoxyribonuclease I,
pubmed-meshheading:1892832-Genes, myc,
pubmed-meshheading:1892832-Humans,
pubmed-meshheading:1892832-Hydrogen Bonding,
pubmed-meshheading:1892832-Mice,
pubmed-meshheading:1892832-Molecular Sequence Data,
pubmed-meshheading:1892832-Nucleic Acid Conformation,
pubmed-meshheading:1892832-Oligonucleotides,
pubmed-meshheading:1892832-Promoter Regions, Genetic,
pubmed-meshheading:1892832-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:1892832-Receptor, Epidermal Growth Factor,
pubmed-meshheading:1892832-Receptor, Insulin
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pubmed:year |
1991
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pubmed:articleTitle |
Binding of triple helix forming oligonucleotides to sites in gene promoters.
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pubmed:affiliation |
Center for Biotechnology, Baylor College of Medicine, Woodlands, Texas 77381.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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