rdf:type |
|
lifeskim:mentions |
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0043393,
umls-concept:C0212320,
umls-concept:C1415470,
umls-concept:C1417715,
umls-concept:C1417716,
umls-concept:C1417717,
umls-concept:C1428360,
umls-concept:C1522492,
umls-concept:C1711351,
umls-concept:C2246376
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pubmed:issue |
5
|
pubmed:dateCreated |
1995-4-4
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pubmed:databankReference |
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pubmed:abstractText |
The CCAAT binding factor CBF is a heteromeric transcription factor, which binds to functional CCAAT motifs in many eukaryotic promoters. cDNAs for the A and B subunits of CBF (CBF-A and CBF-B) and for their yeast homologues HAP3 and HAP2 have been previously isolated, but the purified recombinant CBF-A and CBF-B together are unable to bind to CCAAT motifs in DNA. Here we report the isolation of a cDNA coding for rat CBF-C, demonstrate that recombinant CBF-C is required together with CBF-A and CBF-B to form a CBF-DNA complex, and show that CBF-C is present in this protein-DNA complex together with the other two subunits. We further show that CBF-C allows formation of a complex between the purified recombinant yeast HAP2 and HAP3 polypeptides and a CCAAT-containing DNA and is present in this complex, implying the existence of a CBF-C homologue in yeast. We show that CBF-A and CBF-C interact with each other to form a CBF-A-CBF-C complex and that CBF-B does not interact with CBF-A or CBF-C individually but that it associates with the CBF-A-CBF-C complex. Our results indicate that CBF is a unique evolutionarily conserved DNA binding protein.
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pubmed:grant |
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-1569083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-1592265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-1644837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-1698608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2000400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2123465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2196566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2266139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2329577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2493990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2711183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2826015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2832731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2832732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2850264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-2911757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-3280141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-3349524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-3399893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-3476205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-3547076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-8159696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7878029-8223474
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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/CCAAT-Binding Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Core Binding Factors,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HAP3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1624-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7878029-Amino Acid Sequence,
pubmed-meshheading:7878029-Animals,
pubmed-meshheading:7878029-Base Sequence,
pubmed-meshheading:7878029-CCAAT-Binding Factor,
pubmed-meshheading:7878029-Cloning, Molecular,
pubmed-meshheading:7878029-Core Binding Factors,
pubmed-meshheading:7878029-DNA, Complementary,
pubmed-meshheading:7878029-DNA-Binding Proteins,
pubmed-meshheading:7878029-Fungal Proteins,
pubmed-meshheading:7878029-Macromolecular Substances,
pubmed-meshheading:7878029-Molecular Sequence Data,
pubmed-meshheading:7878029-Neoplasm Proteins,
pubmed-meshheading:7878029-Oligodeoxyribonucleotides,
pubmed-meshheading:7878029-Peptide Mapping,
pubmed-meshheading:7878029-Peptides,
pubmed-meshheading:7878029-Protein Binding,
pubmed-meshheading:7878029-Rats,
pubmed-meshheading:7878029-Recombinant Proteins,
pubmed-meshheading:7878029-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:7878029-Saccharomyces cerevisiae,
pubmed-meshheading:7878029-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:7878029-Transcription Factors
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pubmed:year |
1995
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pubmed:articleTitle |
Recombinant rat CBF-C, the third subunit of CBF/NFY, allows formation of a protein-DNA complex with CBF-A and CBF-B and with yeast HAP2 and HAP3.
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pubmed:affiliation |
Department of Molecular Genetics, University of Texas, M.D. Anderson Cancer Center, Houston 77030.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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