Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
|
pubmed:dateCreated |
1992-9-10
|
pubmed:abstractText |
Full-length cDNA clones for the CBF-A and CBF-B subunits of the CCAAT binding mammalian heteromeric transcription factor (CBF) have previously been isolated from both rat and mouse. Whereas recombinant CBF-B binds to DNA after complementation with a highly purified CBF-A fraction, recombinant CBF-A was unable to bind to DNA after complementation with either purified CBF-B or recombinant CBF-B. However, when recombinant CBF-A, synthesized as a fusion protein with glutathione S-transferase was denatured together with a highly purified fraction containing CBF-A in the presence of 5.5 M guanidine hydrochloride and subsequently renatured, the recombinant CBF-A bound to DNA after complementation with CBF-B. This binding of recombinant CBF-A could not be detected if recombinant CBF-A was not mixed during the denaturation-renaturation process together with the purified fraction containing the 32-kDa CBF-A. Using a Southwestern blot we demonstrated that a polypeptide of approximately 40 kDa, present in the purified CBF-A fraction, bound to DNA after complementation with both recombinant CBF-A and CBF-B. After fractionation of the purified CBF-A preparation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a species of approximately 40 kDa was eluted from the gel and shown to have DNA binding activity after complementation with both recombinant CBF-A and CBF-B. Our results indicate that a third polypeptide, designated CBF-C, forms a tight complex with CBF-A. Together with CBF-A and CBF-B, CBF-C is required for the DNA binding activity of CBF.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCAAT-Enhancer-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
267
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
16574-80
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:1644837-Animals,
pubmed-meshheading:1644837-CCAAT-Enhancer-Binding Proteins,
pubmed-meshheading:1644837-Cloning, Molecular,
pubmed-meshheading:1644837-DNA,
pubmed-meshheading:1644837-DNA-Binding Proteins,
pubmed-meshheading:1644837-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1644837-Immunoblotting,
pubmed-meshheading:1644837-Liver,
pubmed-meshheading:1644837-Macromolecular Substances,
pubmed-meshheading:1644837-Molecular Weight,
pubmed-meshheading:1644837-Protein Denaturation,
pubmed-meshheading:1644837-Rats,
pubmed-meshheading:1644837-Recombinant Fusion Proteins,
pubmed-meshheading:1644837-Transcription Factors
|
pubmed:year |
1992
|
pubmed:articleTitle |
Three different polypeptides are necessary for DNA binding of the mammalian heteromeric CCAAT binding factor.
|
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.
|