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An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B.

Covalent modifications of histone tails play important roles in gene transcription and silencing. We recently identified an ERG ( ets -related gene)-associated protein with a SET (suppressor of variegation, enhancer of zest and trithorax) domain (ESET) that was found to have the activity of a histone H3-specific methyltransferase. In the present study, we investigated the interaction of ESET with other chromatin remodelling factors. We show that ESET histone methyltransferase associates with histone deacetylase 1 (HDAC1) and HDAC2, and that ESET also interacts with the transcription co-repressors mSin3A and mSin3B. Deletion analysis of ESET reveals that an N-terminal region containing a tudor domain is responsible for interaction with mSin3A/B and association with HDAC1/2, and that truncation of ESET enhances its binding to mSin3. When bound to a promoter, ESET represses the transcription of a downstream luciferase reporter gene. This repression by ESET is independent of its histone methyltransferase activity, but correlates with its binding to the mSin3 co-repressors. In addition, the repression can be partially reversed by treatment with the HDAC inhibitor trichostatin A. Taken together, these data suggest that ESET histone methyltransferase can form a large, multi-protein complex(es) with mSin3A/B co-repressors and HDAC1/2 that participates in multiple pathways of transcriptional repression.

Pubmed ID: 12398767


  • Yang L
  • Mei Q
  • Zielinska-Kwiatkowska A
  • Matsui Y
  • Blackburn ML
  • Benedetti D
  • Krumm AA
  • Taborsky GJ
  • Chansky HA


The Biochemical journal

Publication Data

February 1, 2003

Associated Grants

  • Agency: NCI NIH HHS, Id: 1R01CA90941

Mesh Terms

  • Animals
  • Binding Sites
  • Catalytic Domain
  • Cells, Cultured
  • Enzyme Inhibitors
  • Histone Deacetylase 1
  • Histone Deacetylase 2
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases
  • Histone-Lysine N-Methyltransferase
  • Humans
  • Hydroxamic Acids
  • Male
  • Methyltransferases
  • Mice
  • Promoter Regions, Genetic
  • Protein Methyltransferases
  • Protein Structure, Tertiary
  • RNA Splicing
  • Recombinant Proteins
  • Repressor Proteins
  • Testis
  • Transcription Factors
  • Transcription, Genetic
  • Transfection