title: Plant homologs of mammalian MBT-domain protein-regulated KDM1 histone lysine demethylases do not interact with plant Tudor/PWWP/MBT-domain proteins.
abstract: Histone lysine demethylases of the LSD1/KDM1 family play important roles in epigenetic regulation of eukaryotic chromatin, and they are conserved between plants and animals. Mammalian LSD1 is thought to be targeted to its substrates, i.e., methylated histones, by an MBT-domain protein SFMBT1 that represents a component of the LSD1-based repressor complex and binds methylated histones. Because MBT-domain proteins are conserved between different organisms, from animals to plants, we examined whether the KDM1-type histone lysine demethylases KDM1C and FLD of Arabidopsis interact with the Arabidopsis Tudor/PWWP/MBT-domain SFMBT1-like proteins SL1, SL2, SL3, and SL4. No such interaction was detected using the bimolecular fluorescence complementation assay in living plant cells. Thus, plants most likely direct their KDM1 chromatin-modifying enzymes to methylated histones of the target chromatin by a mechanism different from that employed by the mammalian cells.
authors.affiliation: Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY, 11794-5215, USA; Department of Biosciences, COMSATS Institute of Information Technology Islamabad, Park Road, Islamabad, 44000, Pakistan. Electronic address: irfan_sadiq@comsats.edu.pk.
authors.forename: Irfan
authors.initials: I
authors.lastname: Sadiq
authors.affiliation: Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY, 11794-5215, USA. Electronic address: ido.keren@stonybrook.edu.
authors.forename: Ido
authors.initials: I
authors.lastname: Keren
authors.affiliation: Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY, 11794-5215, USA. Electronic address: vitaly.citovsky@stonybrook.edu.
authors.forename: Vitaly
authors.initials: V
authors.lastname: Citovsky
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D006655:Histone Deacetylases / Q000737:chemistry* / Q000378:metabolism*; D056466:Histone Demethylases / Q000737:chemistry* / Q000378:metabolism*; D026161:MADS Domain Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D013045:Species Specificity
chemical_list: D029681:Arabidopsis Proteins; D026161:MADS Domain Proteins; D056466:Histone Demethylases; C479923:flowering locus D protein, Arabidopsis; D006655:Histone Deacetylases
keywords: Arabidopsis; Histone lysine demethylases; KDM1; Tudor/PWWP/MBT domain proteins
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