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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1994-11-10
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pubmed:abstractText |
We constructed a set of deletions upstream of the gcv promoter and analyzed the effects of the deletions on expression of a gcvT-lacZ gene fusion. A deletion that ends at position -313 upstream of the transcription initiation site (+1) results in reduced levels of gcvT-lacZ expression, but the fusion is still inducible by glycine and repressible by purines. A deletion that ends at position -169 results in loss of both GcvA- and Lrp-mediated activation of the gcvT-lacZ fusion. The endpoints of delta -313 and delta -169 also define a site that down-regulates gcvT-lacZ expression two- to threefold. A deletion that ends at position -89 upstream from the transcription initiation site still shows PurR-mediated repression, suggesting that PurR-mediated repression is not by direct interference with the GcvA- and Lrp-mediated regulatory mechanism(s). Gel mobility shift assays and DNase I footprinting showed that Lrp protein binds to multiple sites upstream of the gcv promoter, from about bp -92 to bp -229. The results suggest that the gcv regulatory region is complex, with numerous cis-acting sites that are required for normal gcv expression.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-13278318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-13745383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-1532173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-1917830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-2539360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-2947897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-3023185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-3058703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-3058704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-322281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-344137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-370784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-4552408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-4585091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-4598009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-6162838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-6246368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-6269071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-6275366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-7901196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-8219277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-8349552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-8375392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-8423160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7928983-8429549
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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/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminomethyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethyl and Formyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine-Responsive Regulatory...,
http://linkedlifedata.com/resource/pubmed/chemical/Lrp protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/glycine cleavage system
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
176
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6159-64
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7928983-Amino Acid Oxidoreductases,
pubmed-meshheading:7928983-Aminomethyltransferase,
pubmed-meshheading:7928983-Bacterial Proteins,
pubmed-meshheading:7928983-Base Sequence,
pubmed-meshheading:7928983-Carrier Proteins,
pubmed-meshheading:7928983-DNA Mutational Analysis,
pubmed-meshheading:7928983-DNA-Binding Proteins,
pubmed-meshheading:7928983-Escherichia coli,
pubmed-meshheading:7928983-Escherichia coli Proteins,
pubmed-meshheading:7928983-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:7928983-Glycine,
pubmed-meshheading:7928983-Hydroxymethyl and Formyl Transferases,
pubmed-meshheading:7928983-Leucine-Responsive Regulatory Protein,
pubmed-meshheading:7928983-Molecular Sequence Data,
pubmed-meshheading:7928983-Multienzyme Complexes,
pubmed-meshheading:7928983-Recombinant Fusion Proteins,
pubmed-meshheading:7928983-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:7928983-Sequence Deletion,
pubmed-meshheading:7928983-Transcription Factors,
pubmed-meshheading:7928983-Transferases
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pubmed:year |
1994
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pubmed:articleTitle |
Characterization of the gcv control region from Escherichia coli.
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pubmed:affiliation |
Department of Microbiology, University of Iowa, Iowa City 52242.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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