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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0012854,
umls-concept:C0014653,
umls-concept:C0212320,
umls-concept:C0439855,
umls-concept:C0936012,
umls-concept:C1148673,
umls-concept:C1261552,
umls-concept:C1428360,
umls-concept:C1511658,
umls-concept:C1522492,
umls-concept:C1704259,
umls-concept:C1704675,
umls-concept:C1705987,
umls-concept:C1711351,
umls-concept:C1880022
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pubmed:issue |
47
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pubmed:dateCreated |
1998-12-21
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pubmed:abstractText |
In this study, we used a photocross-linking method to identify specific contact of CCAAT-binding factor (CBF) subunits in a CBF-DNA complex. The analysis showed that all three subunits in the CBF-DNA complex were cross-linked to DNA and that CBF-B and CBF-C were cross-linked more strongly than CBF-A. None of the CBF-A and CBF-C subunits, which together formed a CBF-A/CBF-C heterodimer, were cross-linked without CBF-B; in contrast, CBF-B was cross-linked in the absence of CBF-A/CBF-C. No subunit of heterotrimeric CBF containing DNA-binding domain mutant of either CBF-B or CBF-C was cross-linked to DNA, and interestingly, cross-linking of CBF-B that occurred without CBF-A/CBF-C was inhibited in presence of mutant CBF-C/CBF-A heterodimer. Altogether, these results indicated that the specific DNA contact surface of each CBF subunit is generated as a result of interaction between CBF-B and CBF-A/CBF-C heterodimer and that the three CBF subunits interact interdependently with DNA to form a CBF-DNA complex. Equilibrium interactions among the three CBF subunits and between CBF subunits and DNA were studied by electrophoretic mobility shift assay. This showed that at equilibrium DNA-binding conditions, the CBF-A/CBF-C heterodimer is very stable, but association between CBF-B and CBF-A/CBF-C is very weak. The nature of the association of CBF-B with CBF-A/CBF-C was also revealed by studying the inhibition of CBF-DNA complex formation by the mutant CBF-B. This study indicated that the association between CBF-B and CBF-A/CBF-C is stabilized upon interaction with DNA, a process likely to favor formation of a high-affinity CBF-DNA complex.
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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/Bromodeoxyuridine,
http://linkedlifedata.com/resource/pubmed/chemical/CCAAT-Enhancer-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins
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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
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pubmed:day |
20
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31590-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9813075-Bromodeoxyuridine,
pubmed-meshheading:9813075-CCAAT-Enhancer-Binding Proteins,
pubmed-meshheading:9813075-Cross-Linking Reagents,
pubmed-meshheading:9813075-DNA,
pubmed-meshheading:9813075-DNA-Binding Proteins,
pubmed-meshheading:9813075-Dimerization,
pubmed-meshheading:9813075-Models, Chemical,
pubmed-meshheading:9813075-Mutation,
pubmed-meshheading:9813075-Photochemistry,
pubmed-meshheading:9813075-Protein Binding,
pubmed-meshheading:9813075-Protein Conformation,
pubmed-meshheading:9813075-Surface Properties,
pubmed-meshheading:9813075-Ultraviolet Rays
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pubmed:year |
1998
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pubmed:articleTitle |
Pathway of complex formation between DNA and three subunits of CBF/NF-Y. Photocross-linking analysis of DNA-protein interaction and characterization of equilibrium steps of subunit interaction and dna binding.
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pubmed:affiliation |
Department of Molecular Genetics, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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