Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-4-4
pubmed:databankReference
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.
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
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1624-8
pubmed:dateRevised
2009-11-18
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
pubmed:year
1995
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.
pubmed:affiliation
Department of Molecular Genetics, University of Texas, M.D. Anderson Cancer Center, Houston 77030.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.