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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1993-12-3
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pubmed:abstractText |
The murine Hoxa-4 gene encodes a protein with a homeodomain closely related to those produced by the Antennapedia-like class of Drosophila genes. Drosophila homeodomain proteins can function as transcription factors, binding to several specific DNA sequences. One sequence that is frequently encountered contains a core ATTA motif within a larger consensus sequence, such as CAATTAA. The in vitro synthesized protein product of Hoxa-4 was shown to bind to a subset of restriction fragments of the Hoxa-4 gene itself as determined by gel retardation experiments. Direct examination of the sequences of the fragments bound by Hoxa-4 protein revealed the presence of four regions containing the core ATTA motif. Two regions contained sequences of the CAATTAA class and were located approximately 1 kb upstream from the putative somatic Hoxa-4 promoter and within the intron. Two additional binding sites containing the consensus target sequence involved in autoregulation of Drosophila Deformed gene were identified: one immediately downstream of the putative embryonic transcription start site and one within the intron, respectively. Specific binding of the in vitro produced Hoxa-4 protein to oligonucleotides corresponding to these sequences was observed in gel retardation assays. The same results were obtained with Hoxa-4 protein produced in a Baculovirus expression system. Experiments using oligonucleotides containing base substitutions in positions 1, 3, 4, and 5 in the sequence CAATTAA showed severely reduced binding. The use of truncated mutant Hoxa-4 proteins in gel retardation assays and in transient co-transfection experiments revealed that the intact homeodomain was required for the binding. These results also suggested that the Hoxa-4 gene has the potential to auto-regulate its expression by interacting with the homeodomain binding sites present in the promoter as well as in the intron.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fushi Tarazu Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hoxa4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0730-2312
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:geneSymbol |
Dfd,
HOX3D,
HOX4C,
HOX4D,
HOX6A,
Hox-1.4,
Hox-2.2,
Hox-4.2,
Hox-C,
Hoxa-4,
Hoxb-4,
Hoxb-6,
Hoxd-4,
ftz
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
449-62
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7901228-Amino Acid Sequence,
pubmed-meshheading:7901228-Animals,
pubmed-meshheading:7901228-Base Sequence,
pubmed-meshheading:7901228-Binding Sites,
pubmed-meshheading:7901228-Consensus Sequence,
pubmed-meshheading:7901228-DNA,
pubmed-meshheading:7901228-DNA-Binding Proteins,
pubmed-meshheading:7901228-Fushi Tarazu Transcription Factors,
pubmed-meshheading:7901228-Genes, Homeobox,
pubmed-meshheading:7901228-Homeodomain Proteins,
pubmed-meshheading:7901228-Insect Hormones,
pubmed-meshheading:7901228-Introns,
pubmed-meshheading:7901228-Mice,
pubmed-meshheading:7901228-Molecular Sequence Data,
pubmed-meshheading:7901228-Promoter Regions, Genetic,
pubmed-meshheading:7901228-Protein Binding,
pubmed-meshheading:7901228-Recombinant Fusion Proteins,
pubmed-meshheading:7901228-Transcription, Genetic
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pubmed:year |
1993
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pubmed:articleTitle |
Protein product of the somatic-type transcript of the Hoxa-4 (Hox-1.4) gene binds to homeobox consensus binding sites in its promoter and intron.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, New York 10032.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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