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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2001-8-24
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pubmed:abstractText |
The Drosophila homeodomain protein Fushi Tarazu (Ftz) and its partner, the orphan receptor Ftz-F1, are members of two distinct families of DNA binding transcriptional regulators. Ftz and Ftz-F1 form a novel partnership in vivo as a Hox/orphan receptor heterodimer. Here we show that the murine Ftz-F1 ortholog SF-1 functionally substitutes for Ftz-F1 in vivo, rescuing the defects of ftz-f1 mutants. This finding identified evolutionarily conserved domains of Ftz-F1 as critical for activity of this receptor in vivo. These domains function, at least in part, by mediating direct protein interactions with Ftz. The Ftz-F1 DNA binding domain interacts strongly with Ftz and dramatically facilitates the binding of Ftz to target DNA. This interaction is augmented by a second interaction between the AF-2 domain of Ftz-F1 and the N-terminus of Ftz via an LRALL sequence in Ftz that is reminiscent of LXXLL motifs in nuclear receptor coactivators. We propose that Ftz-F1 serves as a cofactor for Ftz by facilitating the selection of target sites in the genome that contain Ftz/Ftz-F1 composite binding sites. Ftz, on the other hand, influences Ftz-F1 activity by interacting with its AF-2 domain in a manner that mimics a nuclear receptor coactivator.
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pubmed:language |
eng
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pubmed:journal |
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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/Drosophila 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/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Steroidogenic Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ftz protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/nuclear hormone receptor FTZ-F1...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0925-4773
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-53
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11520662-Amino Acid Motifs,
pubmed-meshheading:11520662-Amino Acid Sequence,
pubmed-meshheading:11520662-Animals,
pubmed-meshheading:11520662-Binding Sites,
pubmed-meshheading:11520662-Conserved Sequence,
pubmed-meshheading:11520662-DNA,
pubmed-meshheading:11520662-DNA-Binding Proteins,
pubmed-meshheading:11520662-Drosophila,
pubmed-meshheading:11520662-Drosophila Proteins,
pubmed-meshheading:11520662-Embryo, Nonmammalian,
pubmed-meshheading:11520662-Evolution, Molecular,
pubmed-meshheading:11520662-Fushi Tarazu Transcription Factors,
pubmed-meshheading:11520662-Gene Expression Regulation, Developmental,
pubmed-meshheading:11520662-Homeodomain Proteins,
pubmed-meshheading:11520662-Insect Proteins,
pubmed-meshheading:11520662-Mice,
pubmed-meshheading:11520662-Molecular Sequence Data,
pubmed-meshheading:11520662-Mutation,
pubmed-meshheading:11520662-Phenotype,
pubmed-meshheading:11520662-Protein Binding,
pubmed-meshheading:11520662-Protein Structure, Tertiary,
pubmed-meshheading:11520662-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:11520662-Steroidogenic Factor 1,
pubmed-meshheading:11520662-Transcription, Genetic,
pubmed-meshheading:11520662-Transcription Factors,
pubmed-meshheading:11520662-Zinc Fingers
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pubmed:year |
2001
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pubmed:articleTitle |
The nuclear receptor Ftz-F1 and homeodomain protein Ftz interact through evolutionarily conserved protein domains.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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