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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-8-6
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pubmed:abstractText |
Pur alpha has been identified as a single-stranded DNA binding protein that specifically binds to the purine-rich strand present in the DNA replication initiation zone of the human c-myc gene. We have previously demonstrated that chronic morphine treatment decreases the DNA binding activity of ssCRE-BP (single-stranded cyclic AMP response element-binding protein), which has been shown to be identical to pur alpha by cDNA cloning, and is abundant in the brain. In this report we identified an activator of ssCRE-BP/pur alpha in the brain and characterized it. Although purified ssCRE-BP/pur alpha or its GST-fusion protein exhibited very low DNA binding activities, they were markedly enhanced by including nuclear extract in the binding assay. The enhanced binding activity is trypsin-sensitive, heat-stable and has a molecular weight of approximately 66 kDa. Casein could substitute for the activator and increased the DNA binding activity of ssCRE-BP/pur alpha by one order. A series of deletion mutants were prepared in order to determine the DNA binding and activator interacting domains, and both of them were found to reside in AA 50-215 of ssCRE-BP/pur alpha. These data suggest that the DNA binding activity of ssCRE-BP/pur alpha is augmented by a nuclear protein, which may modulate the ssCRE-BP/pur alpha activity to develop morphine dependence and tolerance.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Biological Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pura protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0197-0186
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45-54
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pubmed:dateRevised |
2005-11-21
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pubmed:meshHeading |
pubmed-meshheading:9185164-Animals,
pubmed-meshheading:9185164-Biological Factors,
pubmed-meshheading:9185164-Caseins,
pubmed-meshheading:9185164-Cell Nucleus,
pubmed-meshheading:9185164-Cerebellum,
pubmed-meshheading:9185164-Cyclic AMP Response Element-Binding Protein,
pubmed-meshheading:9185164-DNA-Binding Proteins,
pubmed-meshheading:9185164-Mice,
pubmed-meshheading:9185164-Molecular Weight,
pubmed-meshheading:9185164-Mutation,
pubmed-meshheading:9185164-Nerve Tissue Proteins,
pubmed-meshheading:9185164-Protein Structure, Tertiary,
pubmed-meshheading:9185164-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
Characterization of a nuclear factor that enhances DNA binding activity of SSCRE-BP/PUR alpha, a single-stranded DNA binding protein.
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pubmed:affiliation |
Department of Pharmacology 1, Osaka University Medical School, Japan.
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pubmed:publicationType |
Journal Article
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