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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6355
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pubmed:dateCreated |
1992-2-18
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pubmed:abstractText |
Positive control of transcription often involves stimulatory protein-protein interactions between regulatory factors and RNA polymerase. Critical steps in the activation process itself are seldom ascribed to protein-DNA distortions. Activator-induced DNA bending is typically assigned a role in binding-site recognition, alterations in DNA loop structures or optimal positioning of the activator for interaction with polymerase. Here we present a transcriptional activation mechanism that does not require a signal-induced DNA bend but rather a receptor-induced untwisting of duplex DNA. The allosterically modulated transcription factor MerR is a repressor and an Hg(II)-responsive activator of bacterial mercury-resistance genes. Escherichia coli RNA polymerase binds to the MerR-promoter complex but cannot proceed to a transcriptionally active open complex until Hg(II) binds to MerR (ref. 6). Chemical nuclease studies show that the activator form, but not the repressor, induces a unique alteration of the helical structure localized at the centre of the DNA-binding site. Data presented here indicate that this Hg-MerR-induced DNA distortion corresponds to a local underwinding of the spacer region of the promoter by about 33 degrees relative to the MerR-operator complex. The magnitude and the direction of the Hg-MerR-induced change in twist angle are consistent with a positive control mechanism involving reorientation of conserved, but suboptimally phased, promoter elements and are consistent with a role for torsional stress in formation of an open complex.
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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/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/MerR protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Mercury
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
355
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
87-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1731201-Allosteric Regulation,
pubmed-meshheading:1731201-Bacterial Proteins,
pubmed-meshheading:1731201-Base Sequence,
pubmed-meshheading:1731201-Binding Sites,
pubmed-meshheading:1731201-DNA, Bacterial,
pubmed-meshheading:1731201-DNA-Binding Proteins,
pubmed-meshheading:1731201-DNA-Directed RNA Polymerases,
pubmed-meshheading:1731201-Escherichia coli,
pubmed-meshheading:1731201-Mercury,
pubmed-meshheading:1731201-Molecular Sequence Data,
pubmed-meshheading:1731201-Plasmids,
pubmed-meshheading:1731201-Promoter Regions, Genetic,
pubmed-meshheading:1731201-Restriction Mapping,
pubmed-meshheading:1731201-Transcription, Genetic
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pubmed:year |
1992
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pubmed:articleTitle |
Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3113.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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