rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
2001-4-12
|
pubmed:abstractText |
Mac1p is a Saccharomyces cerevisiae DNA binding transcription factor that activates genes involved in copper uptake. A copper-induced N-C-terminal intramolecular interaction and copper-independent homodimerization affect its function. Here, we present a functional analysis of Mac1p deletion derivatives that attributes new roles to the second cysteine-rich (REPII) domain of the protein. This domain exhibits the copper-responsive potent transactivation function when assayed independently and, in the context of the entire protein, modulates the efficiency of Mac1p binding to DNA. The efficiency of binding to both copper-response promoter elements can determine the in vivo functionality of Mac1p independent of homodimerization.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
6
|
pubmed:volume |
494
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
38-43
|
pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11297731-Binding Sites,
pubmed-meshheading:11297731-Copper,
pubmed-meshheading:11297731-Cysteine,
pubmed-meshheading:11297731-DNA,
pubmed-meshheading:11297731-Dimerization,
pubmed-meshheading:11297731-Fungal Proteins,
pubmed-meshheading:11297731-Nuclear Proteins,
pubmed-meshheading:11297731-Saccharomyces cerevisiae,
pubmed-meshheading:11297731-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11297731-Trans-Activators,
pubmed-meshheading:11297731-Transcription Factors,
pubmed-meshheading:11297731-Transcriptional Activation
|
pubmed:year |
2001
|
pubmed:articleTitle |
The second cysteine-rich domain of Mac1p is a potent transactivator that modulates DNA binding efficiency and functionality of the protein.
|
pubmed:affiliation |
Foundation for Research and Technology-HELLAS, Institute of Molecular Biology and Biotechnology, Heraklion, Crete, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|