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http://purl.uniprot.org/citations/16258034http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16258034http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16258034http://www.w3.org/2000/01/rdf-schema#comment"Winter-annual accessions of Arabidopsis thaliana are often characterized by a requirement for exposure to the cold of winter to initiate flowering in the spring. The block to flowering prior to cold exposure is due to high levels of the flowering repressor FLOWERING LOCUS C (FLC). Exposure to cold promotes flowering through a process known as vernalization that epigenetically represses FLC expression. Rapid-cycling accessions typically have low levels of FLC expression and therefore do not require vernalization. A screen for mutants in which a winter-annual Arabidopsis is converted to a rapid-cycling type has identified a putative histone H3 methyl transferase that is required for FLC expression. Lesions in this methyl transferase, EARLY FLOWERING IN SHORT DAYS (EFS), result in reduced levels of histone H3 Lys 4 trimethylation in FLC chromatin. EFS is also required for expression of other genes in the FLC clade, such as MADS AFFECTING FLOWERING2 and FLOWERING LOCUS M. The requirement for EFS to permit expression of several FLC clade genes accounts for the ability of efs lesions to suppress delayed flowering due to the presence of FRIGIDA, autonomous pathway mutations, or growth in noninductive photoperiods. efs mutants exhibit pleiotropic phenotypes, indicating that the role of EFS is not limited to the regulation of flowering time."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.org/dc/terms/identifier"doi:10.1105/tpc.105.034645"xsd:string
http://purl.uniprot.org/citations/16258034http://purl.org/dc/terms/identifier"doi:10.1105/tpc.105.034645"xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"He Y."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"He Y."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Kim S.Y."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Kim S.Y."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Noh Y.-S."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Noh Y.-S."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Amasino R."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Amasino R."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Jacob Y."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Jacob Y."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Michaels S."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/author"Michaels S."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/pages"3301-3310"xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/pages"3301-3310"xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/title"Establishment of the vernalization-responsive, winter-annual habit in Arabidopsis requires a putative histone H3 methyl transferase."xsd:string
http://purl.uniprot.org/citations/16258034http://purl.uniprot.org/core/title"Establishment of the vernalization-responsive, winter-annual habit in Arabidopsis requires a putative histone H3 methyl transferase."xsd:string