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http://purl.uniprot.org/citations/16127716http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16127716http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16127716http://www.w3.org/2000/01/rdf-schema#comment"FoxA transcription factors are central regulators of gut development in all animals that have been studied. Here we examine the sole Caenorhabditis elegans FoxA protein, which is called pha-4. We describe the molecular characterization of five pha-4 mutations and characterize their associated phenotypes. Two nonsense mutations are predicted to truncate PHA-4 after the DNA binding domain and remove the conserved carboxyl terminus. Surprisingly, animals harboring these mutations are viable, provided the mutant mRNAs are stabilized by inactivating the nonsense-mediated decay pathway. Two additional nonsense mutations reveal that the DNA binding domain is critical for activity. A missense mutation predicted to alter the PHA-4 amino terminus leads to a dramatic reduction in pha-4 activity even though the protein is expressed appropriately. We suggest that the PHA-4 amino terminus is essential for PHA-4 function in vivo, possibly as a transactivation domain, and can compensate for loss of the carboxyl terminus. We also provide evidence for autoregulation by PHA-4."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.org/dc/terms/identifier"doi:10.1002/dvdy.20550"xsd:string
http://purl.uniprot.org/citations/16127716http://purl.org/dc/terms/identifier"doi:10.1002/dvdy.20550"xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/author"Mango S.E."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/author"Mango S.E."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/author"Updike D.L."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/author"Updike D.L."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/author"Kaltenbach L.S."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/author"Kaltenbach L.S."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/name"Dev. Dyn."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/name"Dev. Dyn."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/pages"346-354"xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/pages"346-354"xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/title"Contribution of the amino and carboxyl termini for PHA-4/FoxA function in Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/title"Contribution of the amino and carboxyl termini for PHA-4/FoxA function in Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/volume"234"xsd:string
http://purl.uniprot.org/citations/16127716http://purl.uniprot.org/core/volume"234"xsd:string
http://purl.uniprot.org/citations/16127716http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16127716
http://purl.uniprot.org/citations/16127716http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16127716
http://purl.uniprot.org/citations/16127716http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16127716
http://purl.uniprot.org/citations/16127716http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16127716