Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1.
Dnmt3b, a DNA methyltransferase, is essential for mammalian development potentially through its transcription repression activity. To comprehend the underlying regulatory mechanism of Dnmt3b, we isolated small ubiquitin-like modifier 1 (SUMO-1) and Ubc9 as Dnmt3b-interacting proteins using yeast two-hybrid screens. Deletion analysis and colocalization experiment demonstrated that Dnmt3b interacts with SUMO-1 ... and Ubc9 at its N-terminal region. We also confirmed the modification of Dnmt3b by SUMO-1 in vivo. These results suggest that sumoylation may constitute a regulation mechanism of Dnmt3b in vivo.
Mesh Terms:
Alternative Splicing, Animals, Binding Sites, Cell Line, DNA (Cytosine-5-)-Methyltransferase, Humans, Ligases, Mice, Protein Processing, Post-Translational, Recombinant Fusion Proteins, SUMO-1 Protein, Sequence Deletion, Transfection, Two-Hybrid System Techniques, Ubiquitin-Conjugating Enzymes
Alternative Splicing, Animals, Binding Sites, Cell Line, DNA (Cytosine-5-)-Methyltransferase, Humans, Ligases, Mice, Protein Processing, Post-Translational, Recombinant Fusion Proteins, SUMO-1 Protein, Sequence Deletion, Transfection, Two-Hybrid System Techniques, Ubiquitin-Conjugating Enzymes
Biochem. Biophys. Res. Commun.
Date: Dec. 14, 2001
PubMed ID: 11735126
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- Interactions 4
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