rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-11-28
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pubmed:abstractText |
In order to investigate whether the 2-amino group of guanine, which lies in the minor groove of the B-form helix, can directly influence DNA flexibility and major groove recognition by proteins we have examined the properties of DNA molecules containing inosine and/or 2,6-diaminopurine (DAP) residues. Appropriately substituted tyrT(A93) DNA fragments were prepared by the polymerase chain reaction. Their mobility in non-denaturing gels was affected, consistent with changed anisotropic flexibility leading to increased curvature due to G-->I substitution and decreased curvature due to replacement of adenine with DAP. Band-shift assays of FIS protein binding revealed facilitated interaction with inosine-containing DNA and markedly reduced binding to DAP-containing DNA, attributable to altered bendability. DNase footprinting experiments confirmed that fewer sites would bind FIS in DAP-containing DNA at a given protein concentration, whereas higher levels of binding occurred with inosine-containing molecules. Thus base substitutions which affect the placement and presence of the purine 2-amino group in the minor groove can affect both the intrinsic curvature and the bendability of DNA.
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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/2,6-diaminopurine,
http://linkedlifedata.com/resource/pubmed/chemical/2-Aminopurine,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Factor For Inversion Stimulation...,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/Inosine,
http://linkedlifedata.com/resource/pubmed/chemical/Integration Host Factors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Tyr
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
253
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-7
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:7473705-2-Aminopurine,
pubmed-meshheading:7473705-Base Sequence,
pubmed-meshheading:7473705-Carrier Proteins,
pubmed-meshheading:7473705-DNA, Bacterial,
pubmed-meshheading:7473705-DNA Footprinting,
pubmed-meshheading:7473705-DNA-Binding Proteins,
pubmed-meshheading:7473705-Factor For Inversion Stimulation Protein,
pubmed-meshheading:7473705-Guanine,
pubmed-meshheading:7473705-Inosine,
pubmed-meshheading:7473705-Integration Host Factors,
pubmed-meshheading:7473705-Molecular Sequence Data,
pubmed-meshheading:7473705-Nucleic Acid Conformation,
pubmed-meshheading:7473705-Promoter Regions, Genetic,
pubmed-meshheading:7473705-RNA, Transfer, Tyr
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pubmed:year |
1995
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pubmed:articleTitle |
Effects of base substitutions on the binding of a DNA-bending protein.
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pubmed:affiliation |
Department of Pharmacology, University of Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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