Source:http://linkedlifedata.com/resource/pubmed/id/10562559
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
2000-1-20
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pubmed:abstractText |
The hinge-region of the lac repressor plays an important role in the models for induction and DNA looping in the lac operon. When lac repressor is bound to a tight-binding symmetric operator, this region forms an alpha-helix that induces bending of the operator. The presence of the hinge-helices is questioned by previous data that suggest that the repressor does not bend the wild-type operator. We show that in the wild-type complex the hinge-helices are formed and the DNA is bent, similar to the symmetric complex. Furthermore, our data show differences in the binding of the DNA binding domains to the half-sites of the wild-type operator and reveal the role of the central base-pair of the wild-type operator in the repressor-operator interaction. The differences in binding to the operator half-sites are incorporated into a model that explains the relative affinities of the repressor for various lac operator sequences that contain left and right half-sites with different spacer lengths.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lac Repressors,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0261-4189
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6472-80
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10562559-Bacterial Proteins,
pubmed-meshheading:10562559-Base Sequence,
pubmed-meshheading:10562559-Cloning, Molecular,
pubmed-meshheading:10562559-Escherichia coli Proteins,
pubmed-meshheading:10562559-Lac Operon,
pubmed-meshheading:10562559-Lac Repressors,
pubmed-meshheading:10562559-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10562559-Nucleic Acid Conformation,
pubmed-meshheading:10562559-Oligodeoxyribonucleotides,
pubmed-meshheading:10562559-Protein Conformation,
pubmed-meshheading:10562559-Repressor Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Hinge-helix formation and DNA bending in various lac repressor-operator complexes.
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pubmed:affiliation |
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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