Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
Corepressor
HDAC4
Histone deacetylase 5
Histone deacetylase 2
HDAC1
HDAC11
Histone code
DOI:
10.1101/gad.14.1.55
Publication Date:
2021-11-15T03:27:24Z
AUTHORS (4)
ABSTRACT
The transcriptional corepressor SMRT functions by mediating the repressive effect of transcription factors involved in diverse signaling pathways. mechanism which represses basal has been proposed to involve indirect recruitment histone deacetylase HDAC1 via adaptor mSin3A. In contrast this model, a two-hybrid screen on SMRT-interacting proteins resulted isolation recently described HDAC5 and new family member termed HDAC7. Molecular biochemical results indicate that interaction is direct vivo evidence colocalizes SMRT, mHDAC5, mHDAC7 distinct nuclear compartment. Surprisingly, HDAC7 can interact with mSin3A yeast mammalian cells, suggesting association multiple repression complexes. Taken together, our provide first SMRT-mediated promoted class I II deacetylases recruit mSin3A-independent fashion.
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