FTZ-Factor1 and Fushi tarazu interact via conserved nuclear receptor and coactivator motifs
To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand‐binding domains (LBDs). The Drosophila FTZ‐Factor1 (FTZ‐F1) protein is a conserved member of the nuclear receptor superfamily, but was previously thought to lack an AF2 motif, a motif that is req...
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| Published in: | The EMBO journal Vol. 20; no. 3; pp. 510 - 519 |
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| Main Authors: | , , , , , , |
| Format: | Journal Article |
| Language: | English |
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Chichester, UK
John Wiley & Sons, Ltd
01-02-2001
Blackwell Publishing Ltd Oxford University Press |
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| Abstract | To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand‐binding domains (LBDs). The Drosophila FTZ‐Factor1 (FTZ‐F1) protein is a conserved member of the nuclear receptor superfamily, but was previously thought to lack an AF2 motif, a motif that is required for ligand and coactivator binding. Here we show that FTZ‐F1 does have an AF2 motif and that it is required to bind a coactivator, the homeodomain‐containing protein Fushi tarazu (FTZ). We also show that FTZ contains an AF2‐interacting nuclear receptor box, the first to be found in a homeodomain protein. Both interaction motifs are shown to be necessary for physical interactions in vitro and for functional interactions in developing embryos. These unexpected findings have important implications for the conserved homologs of the two proteins. |
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| AbstractList | To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand-binding domains (LBDs). The DrosophilaFTZ-Factor1 (FTZ-F1) protein is a conserved member of the nuclear receptor superfamily, but was previously thought to lack an AF2 motif, a motif that is required for ligand and coactivator binding. Here we show that FTZ-F1 does have an AF2 motif and that it is required to bind a coactivator, the homeodomain-containing protein Fushi tarazu (FTZ). We also show that FTZ contains an AF2-interacting nuclear receptor box, the first to be found in a homeodomain protein. Both interaction motifs are shown to be necessary for physical interactions in vitro and for functional interactions in developing embryos. These unexpected findings have important implications for the conserved homologs of the two proteins. To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand-binding domains (LBDs). The Drosophila FTZ-Factor1 (FTZ-F1) protein is a conserved member of the nuclear receptor superfamily, but was previously thought to lack an AF2 motif, a motif that is required for ligand and coactivator binding. Here we show that FTZ-F1 does have an AF2 motif and that it is required to bind a coactivator, the homeodomain-containing protein Fushi tarazu (FTZ). We also show that FTZ contains an AF2-interacting nuclear receptor box, the first to be found in a homeodomain protein. Both interaction motifs are shown to be necessary for physical interactions in vitro and for functional interactions in developing embryos. These unexpected findings have important implications for the conserved homologs of the two proteins. To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand-binding domains (LBDs). The Drosophila FTZ-Factor1 (FTZ-F1) protein is a conserved member of the nuclear receptor superfamily, but was previously thought to lack an AF2 motif, a motif that is required for ligand and coactivator binding. Here we show that FTZ-F1 does have an AF2 motif and that it is required to bind a coactivator, the homeodomain-containing protein Fushi tarazu (FTZ). We also show that FTZ contains an AF2-interacting nuclear receptor box, the first to be found in a homeodomain protein. Both interaction motifs are shown to be necessary for physical interactions in vitro and for functional interactions in developing embryos. These unexpected findings have important implications for the conserved homologs of the two proteins. |
| Author | Krause, Henry M. Schwartz, Carol J.E. Simmonds, Andrew J. Copeland, John W.R. Percival-Smith, Anthony Sampson, Heidi M. Hlousek, Daniela |
| AuthorAffiliation | Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Toronto, Ontario, Canada M5G 1L6 and 1 Department of Zoology, University of Western Ontario, London, Ontario, Canada N6A 5B7 2 Corresponding author e-mail: h.krause@utoronto.ca |
| AuthorAffiliation_xml | – name: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Toronto, Ontario, Canada M5G 1L6 and 1 Department of Zoology, University of Western Ontario, London, Ontario, Canada N6A 5B7 2 Corresponding author e-mail: h.krause@utoronto.ca |
| Author_xml | – sequence: 1 givenname: Carol J.E. surname: Schwartz fullname: Schwartz, Carol J.E. organization: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Ontario, M5G 1L6, Toronto, Canada – sequence: 2 givenname: Heidi M. surname: Sampson fullname: Sampson, Heidi M. organization: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Ontario, M5G 1L6, Toronto, Canada – sequence: 3 givenname: Daniela surname: Hlousek fullname: Hlousek, Daniela organization: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Ontario, M5G 1L6, Toronto, Canada – sequence: 4 givenname: Anthony surname: Percival-Smith fullname: Percival-Smith, Anthony organization: Department of Zoology, University of Western Ontario, Ontario, N6A 5B7, London, Canada – sequence: 5 givenname: John W.R. surname: Copeland fullname: Copeland, John W.R. organization: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Ontario, M5G 1L6, Toronto, Canada – sequence: 6 givenname: Andrew J. surname: Simmonds fullname: Simmonds, Andrew J. organization: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Ontario, M5G 1L6, Toronto, Canada – sequence: 7 givenname: Henry M. surname: Krause fullname: Krause, Henry M. email: h.krause@utoronto.ca organization: Banting and Best Department of Medical Research, University of Toronto and C.H.Best Institute, 112 College Street, Ontario, M5G 1L6, Toronto, Canada |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11157757$$D View this record in MEDLINE/PubMed |
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| Snippet | To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand‐binding domains (LBDs). The Drosophila FTZ‐Factor1... To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand-binding domains (LBDs). The Drosophila FTZ-Factor1... To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand-binding domains (LBDs). The DrosophilaFTZ-Factor1... To activate transcription, most nuclear receptor proteins require coactivators that bind to their ligand-binding domains (LBDs). The Drosophila FTZ-Factor1... |
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| SubjectTerms | Amino Acid Motifs Amino Acid Sequence Animals Base Sequence Binding Sites - genetics Conserved Sequence DNA - genetics DNA Primers - genetics DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Drosophila Drosophila - embryology Drosophila - genetics Drosophila - metabolism Drosophila Proteins Evolution, Molecular FTZ-F1 FTZ-Factor 1 Fushi tarazu Fushi tarazu protein Fushi Tarazu Transcription Factors homeodomain Homeodomain Proteins - chemistry Homeodomain Proteins - genetics Homeodomain Proteins - metabolism In Vitro Techniques Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - metabolism Ligands Molecular Sequence Data nuclear receptor Receptors, Cytoplasmic and Nuclear - chemistry Receptors, Cytoplasmic and Nuclear - genetics Receptors, Cytoplasmic and Nuclear - metabolism Sequence Homology, Amino Acid Steroidogenic Factor 1 Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism |
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| Title | FTZ-Factor1 and Fushi tarazu interact via conserved nuclear receptor and coactivator motifs |
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