Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Line
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Electrophoretic Mobility Shift Assay
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Glutathione Transferase / genetics
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Glutathione Transferase / metabolism
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Humans
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Luciferases / genetics
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Luciferases / metabolism
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Mice
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Microscopy, Fluorescence
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Oligonucleotides / genetics
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Oligonucleotides / metabolism
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Polycomb Repressive Complex 2
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Protein Binding
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Two-Hybrid System Techniques
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Zinc Fingers*
Substances
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DNA-Binding Proteins
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Jarid2 protein, mouse
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Nerve Tissue Proteins
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Oligonucleotides
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Recombinant Fusion Proteins
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Luciferases
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Polycomb Repressive Complex 2
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Glutathione Transferase