Plant homologs of mammalian MBT-domain protein-regulated KDM1 histone lysine demethylases do not interact with plant Tudor/PWWP/MBT-domain proteins
| Autor: | Vitaly Citovsky, Ido Keren, Irfan Sadiq |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
animal structures Arabidopsis Biophysics MADS Domain Proteins Biochemistry Article Histone Deacetylases 03 medical and health sciences 0302 clinical medicine Species Specificity Histone H1 Protein Interaction Mapping Histone H2A Histone code Histone octamer Molecular Biology Histone Demethylases Binding Sites biology Arabidopsis Proteins Cell Biology Protein Structure Tertiary Chromatin 030104 developmental biology Histone Histone methyltransferase biology.protein 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 470:913-916 |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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