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http://purl.uniprot.org/citations/16429262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16429262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16429262http://www.w3.org/2000/01/rdf-schema#comment"In yeast and mammalian systems, it is well established that transcriptional down-regulation by DNA-binding repressors involves core histone deacetylation, mediated by their interaction within a complex containing histone deacetylase (e.g. HDA1), as well as various other proteins (e.g. SIN3, SAP18, SAP30, and RbAp46). Here we identify that a Arabidopsis thaliana gene related in sequence to SAP18, designated AtSAP18, functions in transcription regulation in plants subjected to salt stress. The AtSAP18 loss-of-function mutant is more sensitive to NaCl, and is impaired in chlorophyll synthesis as compared to the wild-type. Using GST pull-down, two-hybrid, and transient transcription assays, we have characterized SAP18 and HDA1 orthologues and provide evidence that SAP18 and HDA1 function as transcriptional repressors. We further demonstrate that they associate with Ethylene-Responsive Element binding Factors (ERFs) to create a hormone-sensitive multimeric repressor complex under conditions of environmental stress. Our results indicate that AtSAP18 functions to link the HDA complex to transcriptional repressors that are bound to chromatin in a sequence-specific manner, thereby providing the specificity of signal transduction accompanying transcriptional repression under stress conditions."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.org/dc/terms/identifier"doi:10.1007/s11103-005-3880-9"xsd:string
http://purl.uniprot.org/citations/16429262http://purl.org/dc/terms/identifier"doi:10.1007/s11103-005-3880-9"xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/author"Galbraith D.W."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/author"Galbraith D.W."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/author"Song C.-P."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/author"Song C.-P."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/pages"241-257"xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/pages"241-257"xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/title"AtSAP18, an orthologue of human SAP18, is involved in the regulation of salt stress and mediates transcriptional repression in Arabidopsis."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/title"AtSAP18, an orthologue of human SAP18, is involved in the regulation of salt stress and mediates transcriptional repression in Arabidopsis."xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/volume"60"xsd:string
http://purl.uniprot.org/citations/16429262http://purl.uniprot.org/core/volume"60"xsd:string
http://purl.uniprot.org/citations/16429262http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16429262
http://purl.uniprot.org/citations/16429262http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16429262
http://purl.uniprot.org/citations/16429262http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16429262
http://purl.uniprot.org/citations/16429262http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16429262
http://purl.uniprot.org/uniprot/O22446http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16429262
http://purl.uniprot.org/uniprot/O80339http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16429262