Nucleic Acids Research, Vol 26, Issue 12 2899-2907, Copyright © 1998 by Oxford University Press
GE Muscat, LJ Burke and M Downes
Repression of transcription by the classical nuclear receptors (e.g. TR,
RAR), the orphan nuclear receptors (e.g. Rev-erbAalpha/beta), Mxi-1 and Mad
bHLH-zip proteins and the oncoproteins PLZF and LAZ3/BCL6 is mediated by
the corepressors N-CoR and SMRT. The interaction of the corepressors with
the components involved in chromatin remodelling, such as the recruiting
proteins Sin3A/B and the histone deacteylases HDAc-1 and RPD3, has been
analysed in detail. The N-CoR/Sin3/HDAc complexes have a key role in the
regulation of cellular proliferation and differentiation. However, the
interaction of these corepressors with the basal transcriptional machinery
has remained obscure. In this study we demonstrated that the
N-terminalrepression domains and the receptor interactiondomains (RID) of
N-CoR and its splice variants, RIP13a and RIP13Delta1, directly interact
with TAFII32 in vivo and in vitro . We show that interaction domain II
within the N-CoR and RIP13a RID is required for the interaction with
TAFII32. We also observed that N-CoR directly interacts with each of the
basal factors, TFIIB and TAFII70, and can simultaneously interact with all
three basal factors in a non-competitive manner. Furthermore, we provide
evidence that suggests the RVR/Rev-erbbeta-corepressor complex also
interacts with the general transcriptional machinery, and that the
physicalassociation of TFIIB with N-CoR also occurs in the presence of
Sin3B and HDAc-1. Interestingly, we observed that N-CoR expression ablated
the functional interaction between TFIIB and TAFII32 that is critical to
the initiation of transcription. In conclusion, this study demonstrates
that the N-terminal repressor region and the C-terminal RIDs are part of
the corepressor contact interface that mediates the interaction with the
general transcription factors, and demonstrates that TAFs can also directly
interact with corepressors to mediate signals from repressors to the basal
machinery. We also suggest that N-CoR interacts with the central components
of the transcriptional initiation process (TFIIB, TAFs) and locks them into
a non-functional complex or conformation that is not conducive to
transcription.
ARTICLES
The corepressor N-CoR and its variants RIP13a and RIP13Delta1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70
University of Queensland, Centre for Molecular and Cellular Biology, Ritchie Research Laboratories, B402A, St Lucia 4072, Queensland, Australia. g.guscat@cmcb.uq.edu.au
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