Source:http://linkedlifedata.com/resource/pubmed/id/11572867
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
48
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| pubmed:dateCreated |
2001-11-23
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| pubmed:abstractText |
CpG-binding protein is a transcriptional activator that exhibits a unique DNA binding specificity for unmethylated CpG motifs. CpG-binding protein contains a cysteine-rich CXXC domain that is conserved in DNA methyltransferase 1, methyl binding domain protein 1, and human trithorax. In vitro DNA binding assays reveal that CpG-binding protein contains a single DNA binding domain comprised of the CXXC domain and a short carboxyl extension. Specific mutation to alanine of individual conserved cysteine residues within the CXXC domain abolishes DNA binding activity. Denaturation/renaturation experiments in the presence of various metal cations demonstrate that the CXXC domain requires zinc for efficient DNA binding activity. Ligand selection of high affinity binding sites from a pool of degenerate oligonucleotides reveals that CpG-binding protein interacts with a variety of sequences that contains the CpG dinucleotide with a consensus binding site of (A/C)CpG(A/C). Mutation of the CpG motif(s) present within ligand-selected oligonucleotides ablates the interaction with CpG-binding protein, and mutation to thymine of the nucleotides flanking the CpG motifs reduces the affinity of CpG-binding protein. Hence, a CpG motif is necessary and sufficient to comprise a binding site for CpG-binding protein, although the immediate flanking sequence affects binding affinity.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
276
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
44669-76
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:11572867-Alanine,
pubmed-meshheading:11572867-Amino Acid Motifs,
pubmed-meshheading:11572867-Amino Acid Sequence,
pubmed-meshheading:11572867-Base Sequence,
pubmed-meshheading:11572867-Binding Sites,
pubmed-meshheading:11572867-Blotting, Western,
pubmed-meshheading:11572867-CpG Islands,
pubmed-meshheading:11572867-Cysteine,
pubmed-meshheading:11572867-DNA,
pubmed-meshheading:11572867-DNA Methylation,
pubmed-meshheading:11572867-Histidine,
pubmed-meshheading:11572867-Humans,
pubmed-meshheading:11572867-Ligands,
pubmed-meshheading:11572867-Molecular Sequence Data,
pubmed-meshheading:11572867-Mutagenesis, Site-Directed,
pubmed-meshheading:11572867-Mutation,
pubmed-meshheading:11572867-Oligonucleotides,
pubmed-meshheading:11572867-Plasmids,
pubmed-meshheading:11572867-Protein Binding,
pubmed-meshheading:11572867-Protein Denaturation,
pubmed-meshheading:11572867-Protein Folding,
pubmed-meshheading:11572867-Protein Structure, Tertiary,
pubmed-meshheading:11572867-Sequence Homology, Amino Acid,
pubmed-meshheading:11572867-Transcriptional Activation,
pubmed-meshheading:11572867-Zinc
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| pubmed:year |
2001
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| pubmed:articleTitle |
Identification and characterization of the DNA binding domain of CpG-binding protein.
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| pubmed:affiliation |
Herman B Wells Center for Pediatric Research, Section of Pediatric Hematology/Oncology and the Department of Pediatrics, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|