Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-3-11
pubmed:abstractText
RecA protein formed a stable triplex from a 33 bp duplex oligonucleotide and a circular plus strand of M13 DNA when a hairpin connection at the proximal end of the homologous duplex oligonucleotide blocked displacement of the 5' end of its own plus strand. An oligonucleotide with a hairpin connection at the other end yielded five times fewer joints that survived deproteinization, and an ordinary duplex oligonucleotide yielded none. The stability of the three-stranded structure was not attributable to exonucleolytic nibbling of the 3' end of the hairpin oligonucleotide, which could generate a region of stable duplex DNA. In the triplexes, the hairpin duplex became more accessible to copper phenanthroline, exhibited novel sites of cleavage by DNase I, and resisted digestion by Escherichia coli exonuclease I. The enzymatic methylation of only two residues at N-6 adenine and two at N-4 cytosine in the hairpin duplex prior to the pairing reaction lowered the tm of triplexes by 8 deg.C, whereas extensive methylation at N-7 guanine by dimethyl sulfate had no effect. These results are discussed in relation to possible models of triplex DNA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
229
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
328-43
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed-meshheading:8381491-Adenine, pubmed-meshheading:8381491-Base Sequence, pubmed-meshheading:8381491-Cytosine, pubmed-meshheading:8381491-DNA, Bacterial, pubmed-meshheading:8381491-DNA, Single-Stranded, pubmed-meshheading:8381491-Escherichia coli, pubmed-meshheading:8381491-Exonucleases, pubmed-meshheading:8381491-Guanine, pubmed-meshheading:8381491-Hydrogen Bonding, pubmed-meshheading:8381491-Kinetics, pubmed-meshheading:8381491-Methylation, pubmed-meshheading:8381491-Molecular Sequence Data, pubmed-meshheading:8381491-Molecular Structure, pubmed-meshheading:8381491-Nucleic Acid Conformation, pubmed-meshheading:8381491-Oligodeoxyribonucleotides, pubmed-meshheading:8381491-Phenanthrolines, pubmed-meshheading:8381491-Rec A Recombinases, pubmed-meshheading:8381491-Substrate Specificity, pubmed-meshheading:8381491-Temperature
pubmed:year
1993
pubmed:articleTitle
Homologous recognition and triplex formation promoted by RecA protein between duplex oligonucleotides and single-stranded DNA.
pubmed:affiliation
Department of Genetics, Yale University School of Medicine, New Haven, CT 06510.
pubmed:publicationType
Journal Article