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rdf:type |
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lifeskim:mentions |
umls-concept:C0009968,
umls-concept:C0017262,
umls-concept:C0017337,
umls-concept:C0038838,
umls-concept:C0040648,
umls-concept:C0043393,
umls-concept:C0043481,
umls-concept:C0185117,
umls-concept:C1413931,
umls-concept:C1515877,
umls-concept:C1879547,
umls-concept:C2911684
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pubmed:issue |
19
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pubmed:dateCreated |
1991-10-31
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pubmed:abstractText |
Copper, zinc superoxide dismutase (SOD1 gene product) (superoxide:superoxide oxidoreductase, EC 1.15.1.1) is a copper-containing enzyme that functions to prevent oxygen toxicity. In the yeast Saccharomyces cerevisiae, copper levels exert some control over the level of SOD1 expression. We show that the ACE1 transcriptional activator protein, which is responsible for the induction of yeast metallothionein (CUP1) in response to copper, also controls the SOD1 response to copper. A single binding site for ACE1 is present in the SOD1 promoter region, as demonstrated by DNase I protection and methylation interference experiments, and is highly homologous to a high-affinity ACE1 binding site in the CUP1 promoter. The functional importance of this DNA-protein interaction is demonstrated by the facts that (i) copper induction of SOD1 mRNA does not occur in a strain lacking ACE1 and (ii) it does not occur in a strain containing a genetically engineered SOD1 promoter that lacks a functional ACE1 binding site.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-1706459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-1986241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-1991520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-1996089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2167439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2180912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2199796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2403543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2403647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2545701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2643107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2651899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2831994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-2992473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3011417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3013982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3026915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3043194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3052856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3224824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3290902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3312986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3315461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3521218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3537699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3546314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-3896935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-4590469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924315-6386805
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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/CUP2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metallothionein,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:geneSymbol |
ACE1,
CUP1,
SOD1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8558-62
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1924315-Base Sequence,
pubmed-meshheading:1924315-Blotting, Northern,
pubmed-meshheading:1924315-Copper,
pubmed-meshheading:1924315-DNA, Fungal,
pubmed-meshheading:1924315-DNA-Binding Proteins,
pubmed-meshheading:1924315-Gene Expression Regulation, Fungal,
pubmed-meshheading:1924315-Metallothionein,
pubmed-meshheading:1924315-Molecular Sequence Data,
pubmed-meshheading:1924315-Promoter Regions, Genetic,
pubmed-meshheading:1924315-RNA, Fungal,
pubmed-meshheading:1924315-RNA, Messenger,
pubmed-meshheading:1924315-Saccharomyces cerevisiae,
pubmed-meshheading:1924315-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:1924315-Superoxide Dismutase,
pubmed-meshheading:1924315-Transcription, Genetic,
pubmed-meshheading:1924315-Transcription Factors
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pubmed:year |
1991
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pubmed:articleTitle |
ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of California, Los Angeles 90024-1569.
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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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