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

The Biochemical journal | Feb 1, 2003

http://www.ncbi.nlm.nih.gov/pubmed/12398767

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 RIS Download

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

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Associated grants

  • Agency: NCI NIH HHS, Id: 1R01CA90941

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