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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1994-8-30
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pubmed:databankReference |
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pubmed:abstractText |
Expression of the nitrogen catabolic genes in Saccharomyces cerevisiae, including those of the gamma-aminobutyric acid (UGA) and allantoin (DAL) pathways, is regulated positively by the GLN3 protein and negatively by the DAL80 protein. The deduced sequences of the DAL80 and GLN3 proteins contain a zinc finger motif homologous to those shown to bind GATA sequences. In addition, DAL80 protein has been directly shown to bind to a pair of GATA-containing sequences (URSGATA) in vitro, and a pair of GATA-containing sequences (UASNTR) is required for GLN3-dependent transcriptional activation in a heterologous expression vector. We demonstrate here that the GATA-containing sites upstream of UGA4 required for optimal GLN3-dependent transcriptional activation also mediate DAL80 protein binding in vitro and DAL80-responsive regulation in vivo.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1406646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1525858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1579492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1682800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1860815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1944286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-1970293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2137552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2190186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2204806,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2225071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2249770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2276623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2406136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-2651902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-3327750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-6152012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-6310325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-6336730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-6757722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-8332909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-8376332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-8416910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8045902-8455553
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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/4-Aminobutyrate Transaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Allantoin,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DAL80 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GABA Plasma Membrane Transport...,
http://linkedlifedata.com/resource/pubmed/chemical/GATA Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/GLN3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Organic Anion Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/UGA4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-Aminobutyric Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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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:geneSymbol |
UGA1,
UGA4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4718-25
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8045902-4-Aminobutyrate Transaminase,
pubmed-meshheading:8045902-Allantoin,
pubmed-meshheading:8045902-Base Sequence,
pubmed-meshheading:8045902-Carrier Proteins,
pubmed-meshheading:8045902-DNA-Binding Proteins,
pubmed-meshheading:8045902-Fungal Proteins,
pubmed-meshheading:8045902-GABA Plasma Membrane Transport Proteins,
pubmed-meshheading:8045902-GATA Transcription Factors,
pubmed-meshheading:8045902-Gene Expression Regulation, Fungal,
pubmed-meshheading:8045902-Membrane Transport Proteins,
pubmed-meshheading:8045902-Molecular Sequence Data,
pubmed-meshheading:8045902-Organic Anion Transporters,
pubmed-meshheading:8045902-Protein Binding,
pubmed-meshheading:8045902-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:8045902-Repressor Proteins,
pubmed-meshheading:8045902-Saccharomyces cerevisiae,
pubmed-meshheading:8045902-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8045902-Transcription, Genetic,
pubmed-meshheading:8045902-Transcription Factors,
pubmed-meshheading:8045902-gamma-Aminobutyric Acid
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pubmed:year |
1994
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pubmed:articleTitle |
The UGA4 UASNTR site required for GLN3-dependent transcriptional activation also mediates DAL80-responsive regulation and DAL80 protein binding in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of Tennessee, Memphis 38163.
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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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