
Jumonij (JMJ)/Jarid2 plays important roles in embryonic development and functions as a transcriptional repressor. Using yeast two‐hybrid screening, we have identified a cofactor of JMJ, the zinc finger protein 496 (Zfp496) that contains a SCAN, KRAB and zinc finger domain. Our molecular analyses indicate that Zfp496 functions as a transcriptional activator. Further, Zfp496 inhibits the transcriptional repression of JMJ and JMJ represses the transcriptional activation of Zfp496. This study demonstrates that JMJ physically and functionally interacts with Zfp496, which will provide important insights into endogenous target gene regulation by both factors.
zfp496, Recombinant Fusion Proteins, Oligonucleotides, Polycomb Repressive Complex 2, Heart, Electrophoretic Mobility Shift Assay, Nerve Tissue Proteins, Zinc Fingers, Development, Jumonji, Cell Line, DNA-Binding Proteins, Mice, Microscopy, Fluorescence, Two-Hybrid System Techniques, Animals, Humans, Luciferases, Transcription, Glutathione Transferase, Protein Binding
zfp496, Recombinant Fusion Proteins, Oligonucleotides, Polycomb Repressive Complex 2, Heart, Electrophoretic Mobility Shift Assay, Nerve Tissue Proteins, Zinc Fingers, Development, Jumonji, Cell Line, DNA-Binding Proteins, Mice, Microscopy, Fluorescence, Two-Hybrid System Techniques, Animals, Humans, Luciferases, Transcription, Glutathione Transferase, Protein Binding
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