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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
40
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pubmed:dateCreated |
1998-11-4
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pubmed:abstractText |
Cruciform DNA has been implicated in the initiation of DNA replication. Recently, we identified and purified from human (HeLa) cells a protein, CBP, with binding specificity for cruciform DNA. We have reported previously that the CBP activity sediments at approximately 66 kDa in a glycerol gradient. Here, photochemical cross-linking studies and Southwestern analyses confirm that a 70 kDa polypeptide interacts specifically with cruciform DNA. Microsequence analysis of tryptic peptides of the 70 kDa CBP reveals that it is 100% homologous to the 14-3-3 family of proteins and shows that CBP contains the epsilon, beta, gamma, and zeta isoforms of the 14-3-3 family. In addition to polypeptides with the characteristic molecular mass of 14-3-3 proteins (30 and 33 kDa), CBP also contains a polypeptide of 35 kDa which is recognized by an antibody specific for the epsilon isoform of 14-3-3. Cruciform-specific binding activity is also detected in 14-3-3 proteins purified from sheep brain. Immunofluorescene studies confirm the presence of the epsilon, beta, and zeta isoforms of 14-3-3 proteins in the nuclei of HeLa cells. The 14-3-3 family of proteins has been implicated in cell cycle control, and members of this family have been shown to interact with various signaling proteins. Cruciform binding is a new activity associated with the 14-3-3 family.
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/chitin-binding protein 21...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
|
pubmed:volume |
37
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
14317-25
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9760269-14-3-3 Proteins,
pubmed-meshheading:9760269-Amino Acid Sequence,
pubmed-meshheading:9760269-Animals,
pubmed-meshheading:9760269-Bacterial Proteins,
pubmed-meshheading:9760269-Base Sequence,
pubmed-meshheading:9760269-Brain Chemistry,
pubmed-meshheading:9760269-Carrier Proteins,
pubmed-meshheading:9760269-Cell Nucleus,
pubmed-meshheading:9760269-DNA-Binding Proteins,
pubmed-meshheading:9760269-HeLa Cells,
pubmed-meshheading:9760269-Humans,
pubmed-meshheading:9760269-Isomerism,
pubmed-meshheading:9760269-Molecular Sequence Data,
pubmed-meshheading:9760269-Nucleic Acid Conformation,
pubmed-meshheading:9760269-Photochemistry,
pubmed-meshheading:9760269-Proteins,
pubmed-meshheading:9760269-Sheep,
pubmed-meshheading:9760269-Tyrosine 3-Monooxygenase,
pubmed-meshheading:9760269-Ultraviolet Rays
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pubmed:year |
1998
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pubmed:articleTitle |
Human cruciform binding protein belongs to the 14-3-3 family.
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pubmed:affiliation |
McGill Cancer Centre, McGill University, Montréal, Québec, Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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