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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
29
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pubmed:dateCreated |
1995-8-22
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pubmed:abstractText |
Equilibrium and kinetic rate constants were determined for the binding of the initiator protein DnaA of Escherichia coli to its binding site, the non-palindromic 9-bp DnaA box, using gel retardation techniques. The dissociation constant for specific binding was between 1 and 50 nM for individual DnaA boxes on 21-bp double-stranded oligonucleotides. Only DnaA boxes of the sequence TT(A/T)TNCACA resulted in specific fragment retention. Both the 9-bp consensus sequence and flanking sequences determined the binding efficiency. One DnaA monomer was found to bind to a DnaA box and to induce a bend of about 40 degrees.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17622-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7615570-Bacterial Proteins,
pubmed-meshheading:7615570-Base Sequence,
pubmed-meshheading:7615570-Binding Sites,
pubmed-meshheading:7615570-DNA,
pubmed-meshheading:7615570-DNA Replication,
pubmed-meshheading:7615570-DNA-Binding Proteins,
pubmed-meshheading:7615570-Escherichia coli,
pubmed-meshheading:7615570-Kinetics,
pubmed-meshheading:7615570-Molecular Sequence Data
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pubmed:year |
1995
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pubmed:articleTitle |
Interaction of the initiator protein DnaA of Escherichia coli with its DNA target.
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pubmed:affiliation |
Max-Planck-Institut für Molekulare Genetik, Berlin-Dahlem, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|