Linked Life Data

7824276

Source:http://linkedlifedata.com/resource/pubmed/id/7824276

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-2-14
pubmed:abstractText
The tumor suppressor protein p53 is a metal-binding transcription factor whose conformation and function are altered by mutation in cancers. Using murine p53 translated in vitro, we report here that concentrations of copper within the physiological range (< 30 microM) alter the conformation of wild-type p53 and inhibit sequence-specific DNA-binding. Direct binding of copper to p53 in the form of Cu(I) was demonstrated by Electron Spin Resonance using a purified recombinant protein containing residues 1-343 of murine wild-type p53 fused to E. coli maltose binding protein. Moreover, protection against the effect of Cu(II) sulfate was achieved by the Cu(I)-specific chelator bathocuproinedisulfonic acid but not by scavengers of reactive oxygen species, suggesting that alteration of p53 by copper depends upon a Cu(II)/Cu(I) redox mechanism, but does not require the production of reactive oxygen species. Thus copper at physiological concentrations can interact with wild-type p53 and affect its DNA-binding capacity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Modulation by copper of p53 conformation and sequence-specific DNA binding: role for Cu(II)/Cu(I) redox mechanism.
pubmed:affiliation
Department of Biology, University of York, Heslington, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't