Abstract
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.
(c)2001 Elsevier Science.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alternative Splicing
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Animals
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Binding Sites
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Cell Line
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DNA (Cytosine-5-)-Methyltransferases / chemistry*
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DNA (Cytosine-5-)-Methyltransferases / genetics
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DNA (Cytosine-5-)-Methyltransferases / metabolism*
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DNA Methyltransferase 3B
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Humans
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In Vitro Techniques
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Ligases / genetics
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Ligases / metabolism*
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Mice
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Protein Processing, Post-Translational
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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SUMO-1 Protein / genetics
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SUMO-1 Protein / metabolism*
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Sequence Deletion
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Transfection
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Two-Hybrid System Techniques
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Ubiquitin-Conjugating Enzymes*
Substances
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Recombinant Fusion Proteins
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SUMO-1 Protein
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DNA (Cytosine-5-)-Methyltransferases
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Ubiquitin-Conjugating Enzymes
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Ligases
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ubiquitin-conjugating enzyme UBC9