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http://purl.uniprot.org/citations/11247607http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11247607http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11247607http://www.w3.org/2000/01/rdf-schema#comment"Homeodomain-leucine zipper (HDZip) proteins constitute a large family of transcription factors apparently unique to plants. In this report we characterize the DNA-binding and dimerization preferences in vitro of class I HDZip proteins. Using gel-exclusion chromatography and in vitro protein binding assays we demonstrate that the HDZip class I protein ATHB5 forms a homodimeric complex in solution. Consistent with this finding we have demonstrated the sequence-specific interaction of ATHB5 with a 9 bp pseudopalindromic DNA sequence, CAATNATTG, composed of two half-sites overlapping at a central position, by use of a PCR-assisted binding-site selection assay and competitive EMSA experiments. A majority of other known members of HDZip class I interacted with similar DNA sequences, but differed in their preference for A/T versus G/C in the central position of the binding site. Selective heterodimerization in vitro was demonstrated between ATHB5 and different class I HDZip proteins. Heterodimer formation between class I HDZip proteins is of potential functional significance for the integration of information from different signalling pathways in the control of plant development."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.org/dc/terms/identifier"doi:10.1023/a:1006423324025"xsd:string
http://purl.uniprot.org/citations/11247607http://purl.org/dc/terms/identifier"doi:10.1023/a:1006423324025"xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/author"Engstroem P."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/author"Engstroem P."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/author"Johannesson H."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/author"Johannesson H."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/pages"63-73"xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/pages"63-73"xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/title"DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription factors in vitro."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/title"DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription factors in vitro."xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/volume"45"xsd:string
http://purl.uniprot.org/citations/11247607http://purl.uniprot.org/core/volume"45"xsd:string
http://purl.uniprot.org/citations/11247607http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11247607
http://purl.uniprot.org/citations/11247607http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11247607
http://purl.uniprot.org/citations/11247607http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11247607
http://purl.uniprot.org/citations/11247607http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11247607