Linked Life Data

1633174

Source:http://linkedlifedata.com/resource/pubmed/id/1633174

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1992-8-25
pubmed:abstractText
N-terminal fragments of ACE1 protein spanning residues 1-122 or 1-110, termed ACE1(122*) and ACE1(110*), respectively, were investigated in regard to their metal- and double-stranded DNA-binding properties. Band mobility shift assays showed that binding to a specific oligonucleotide (termed UASc), containing two ACE1(122*) binding sites, requires the presence of Cu(I) or Ag(I) but does not occur in the presence of divalent metal ions. Both the Ag(I) and the Cu(I) forms of ACE1(122*) were characterized spectroscopically. The Tyr and metal cluster luminescence emission of Cu-ACE1(122*) was specifically quenched by the oligonucleotide UAScL, but not by an oligonucleotide of the same length and base composition but scrambled sequence. The room-temperature luminescence of Cu(I)-ACE1(122*) was assigned to a phosphorescence emission, on the basis of its long-lived luminescence of approximately 3.5 microseconds. We report the first observation of a Ag(I) metal cluster in solution for Ag(I)-ACE1(122*), which was found to exhibit a quantum yield and average luminescence lifetime that are ca. 6% of that of Cu(I)-ACE1(122*). The three-dimensional structure brought about by the binding of either metal ion appears to be very similar, since dynamic tyrosine fluorescence lifetime measurements, as well as circular dichroism spectra, were nearly identical for Cu- and Ag-ACE1(122*). Based on these results, we present a hypothetical model for the structure of the metal cluster in this class of proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
31
pubmed:geneSymbol
ACE1, CUP2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6617-26
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1633174-Base Sequence, pubmed-meshheading:1633174-Binding Sites, pubmed-meshheading:1633174-Circular Dichroism, pubmed-meshheading:1633174-Copper, pubmed-meshheading:1633174-DNA-Binding Proteins, pubmed-meshheading:1633174-Fungal Proteins, pubmed-meshheading:1633174-Luminescent Measurements, pubmed-meshheading:1633174-Molecular Sequence Data, pubmed-meshheading:1633174-Oligodeoxyribonucleotides, pubmed-meshheading:1633174-Protein Conformation, pubmed-meshheading:1633174-Recombinant Proteins, pubmed-meshheading:1633174-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:1633174-Saccharomyces cerevisiae, pubmed-meshheading:1633174-Saccharomyces cerevisiae Proteins, pubmed-meshheading:1633174-Silver, pubmed-meshheading:1633174-Spectrophotometry, Ultraviolet, pubmed-meshheading:1633174-Transcription Factors, pubmed-meshheading:1633174-Tryptophan
pubmed:year
1992
pubmed:articleTitle
Characterization of the copper- and silver-thiolate clusters in N-terminal fragments of the yeast ACE1 transcription factor capable of binding to its specific DNA recognition sequence.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Maryland, Baltimore County 21228.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't