Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1

Biochem Biophys Res Commun. 2001 Dec 14;289(4):862-8. doi: 10.1006/bbrc.2001.6057.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing
  • Animals
  • Binding Sites
  • Cell Line
  • DNA (Cytosine-5-)-Methyltransferases / chemistry*
  • DNA (Cytosine-5-)-Methyltransferases / genetics
  • DNA (Cytosine-5-)-Methyltransferases / metabolism*
  • DNA Methyltransferase 3B
  • Humans
  • In Vitro Techniques
  • Ligases / genetics
  • Ligases / metabolism*
  • Mice
  • Protein Processing, Post-Translational
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • SUMO-1 Protein / genetics
  • SUMO-1 Protein / metabolism*
  • Sequence Deletion
  • Transfection
  • Two-Hybrid System Techniques
  • Ubiquitin-Conjugating Enzymes*

Substances

  • Recombinant Fusion Proteins
  • SUMO-1 Protein
  • DNA (Cytosine-5-)-Methyltransferases
  • Ubiquitin-Conjugating Enzymes
  • Ligases
  • ubiquitin-conjugating enzyme UBC9