Statements in which the resource exists as a subject.
PredicateObject
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.
pubmed:language
eng
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
pubmed:meshHeading
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.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't