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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4954
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pubmed:dateCreated |
1990-5-25
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pubmed:abstractText |
The nitrogen regulatory protein NtrC of enteric bacteria activates transcription of the glnA gene by catalyzing isomerization of closed complexes between RNA polymerase and the glnA promoter to open complexes. NtrC binds to sites upstream of glnA that have properties of eukaryotic transcriptional enhancers. NtrC-binding sites were found to facilitate open complex formation when these sites and the glnA promoter were located on different rings of a singly linked catenane, but not when the two rings were decatenated. The results provide evidence that NtrC contacts RNA polymerase-promoter complexes in a process mediated by formation of a DNA loop. NtrC-binding sites serve to tether NtrC near the glnA promoter, thereby increasing the frequency of collisions between NtrC and polymerase-promoter complexes.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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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, Superhelical,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Transposable Elements,
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/Glutamate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/PII Nitrogen Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transposases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
248
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
486-90
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1970441-Bacterial Proteins,
pubmed-meshheading:1970441-Binding Sites,
pubmed-meshheading:1970441-DNA, Bacterial,
pubmed-meshheading:1970441-DNA, Superhelical,
pubmed-meshheading:1970441-DNA Transposable Elements,
pubmed-meshheading:1970441-DNA-Binding Proteins,
pubmed-meshheading:1970441-DNA-Directed RNA Polymerases,
pubmed-meshheading:1970441-Enhancer Elements, Genetic,
pubmed-meshheading:1970441-Glutamate-Ammonia Ligase,
pubmed-meshheading:1970441-Nucleotidyltransferases,
pubmed-meshheading:1970441-PII Nitrogen Regulatory Proteins,
pubmed-meshheading:1970441-Plasmids,
pubmed-meshheading:1970441-Promoter Regions, Genetic,
pubmed-meshheading:1970441-Templates, Genetic,
pubmed-meshheading:1970441-Trans-Activators,
pubmed-meshheading:1970441-Transcription, Genetic,
pubmed-meshheading:1970441-Transcription Factors,
pubmed-meshheading:1970441-Transposases
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pubmed:year |
1990
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pubmed:articleTitle |
A bacterial enhancer functions to tether a transcriptional activator near a promoter.
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pubmed:affiliation |
Department of Plant Pathology, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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