rdf:type |
|
lifeskim:mentions |
umls-concept:C0012854,
umls-concept:C0030943,
umls-concept:C0037791,
umls-concept:C0086860,
umls-concept:C0205147,
umls-concept:C0205250,
umls-concept:C0217359,
umls-concept:C0332256,
umls-concept:C1158830,
umls-concept:C1167622,
umls-concept:C1305923
|
pubmed:issue |
3
|
pubmed:dateCreated |
1992-9-10
|
pubmed:abstractText |
The sigma 70 subunit of E. coli RNA polymerase is required for sequence-specific recognition of promoter DNA. Genetic studies and sequence analysis have indicated that sigma 70 contains two specific DNA-binding domains that recognize the two conserved portions of the prokaryotic promoter. However, intact sigma 70 does not bind to DNA. Using C-terminal and internal polypeptides of sigma 70, carrying one or both putative DNA-binding domains, we demonstrate that sigma 70 does contain two DNA-binding domains, but that N-terminal sequences inhibit the ability of intact sigma 70 to bind to DNA. Thus, we propose that sigma 70 is a sequence-specific DNA-binding protein that normally functions through an allosteric interaction with the core subunits of RNA polymerase.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
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/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA polymerase sigma 70,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sigma Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
0092-8674
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
7
|
pubmed:volume |
70
|
pubmed:geneSymbol |
rpoD
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
501-12
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1643661-Bacterial Proteins,
pubmed-meshheading:1643661-Binding Sites,
pubmed-meshheading:1643661-DNA, Bacterial,
pubmed-meshheading:1643661-DNA-Binding Proteins,
pubmed-meshheading:1643661-DNA-Directed RNA Polymerases,
pubmed-meshheading:1643661-Escherichia coli,
pubmed-meshheading:1643661-Glutathione,
pubmed-meshheading:1643661-Glutathione Transferase,
pubmed-meshheading:1643661-Mutagenesis, Site-Directed,
pubmed-meshheading:1643661-Peptides,
pubmed-meshheading:1643661-Plasmids,
pubmed-meshheading:1643661-Promoter Regions, Genetic,
pubmed-meshheading:1643661-Recombinant Fusion Proteins,
pubmed-meshheading:1643661-Sigma Factor
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pubmed:year |
1992
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pubmed:articleTitle |
Polypeptides containing highly conserved regions of transcription initiation factor sigma 70 exhibit specificity of binding to promoter DNA.
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pubmed:affiliation |
Department of Bacteriology, University of Wisconsin, Madison 53706.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|