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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
1990-7-2
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pubmed:abstractText |
The binding of a synthetic four-way junction in DNA by T4 endonuclease VII has been studied using gel retardation and footprint analysis. Two specific protein-DNA complexes have been observed, but only one is stable in the presence of moderate concentrations of salt. The footprint of T4 endonuclease VII in the salt-resistant complex has been probed using hydroxyl radicals generated by the reaction of iron(II)/EDTA with hydrogen peroxide. The hydroxyl radical cleavage pattern indicates protection of approximately 5 residues in two strands that are diametrically opposed across the junction point.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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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 |
5
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9285-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2160971-Base Sequence,
pubmed-meshheading:2160971-Binding Sites,
pubmed-meshheading:2160971-DNA,
pubmed-meshheading:2160971-Edetic Acid,
pubmed-meshheading:2160971-Endodeoxyribonucleases,
pubmed-meshheading:2160971-Ferrous Compounds,
pubmed-meshheading:2160971-Hydrogen Peroxide,
pubmed-meshheading:2160971-Hydroxides,
pubmed-meshheading:2160971-Hydroxyl Radical,
pubmed-meshheading:2160971-Macromolecular Substances,
pubmed-meshheading:2160971-Molecular Sequence Data,
pubmed-meshheading:2160971-Molecular Weight,
pubmed-meshheading:2160971-Nucleic Acid Conformation
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pubmed:year |
1990
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pubmed:articleTitle |
Interaction of a four-way junction in DNA with T4 endonuclease VII.
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pubmed:affiliation |
Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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