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PMID: 9611234 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The corepressor N-CoR and its variants RIP13a and RIP13Delta1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70.

Nucleic acids research ·Vol. 26 ·No. 12 ·1998-06-15 ·Pages 2899-907

Muscat GE, Burke LJ, Downes M

Abstract

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.

MeSH Terms
Animals DNA-Binding Proteins/metabolism Histone Deacetylase 1 Histone Deacetylases/metabolism Nerve Tissue Proteins/metabolism Nuclear Proteins/genetics,metabolism Nuclear Receptor Co-Repressor 1 Protein Binding Receptors, Cytoplasmic and Nuclear/metabolism Receptors, Thyroid Hormone Recombinant Fusion Proteins Repressor Proteins/genetics,metabolism TATA-Binding Protein Associated Factors Transcription Factor TFIIB Transcription Factor TFIID Transcription Factors/genetics,metabolism Transcription Factors, TFII/metabolism Transcription, Genetic/physiology
Chemicals
DNA-Binding Proteins NCOR1 protein, human Nerve Tissue Proteins Nuclear Proteins Nuclear Receptor Co-Repressor 1 Receptors, Cytoplasmic and Nuclear Receptors, Thyroid Hormone Recombinant Fusion Proteins Repressor Proteins TAF6 protein, human TAF9 protein, human TATA-Binding Protein Associated Factors Transcription Factor TFIIB Transcription Factor TFIID Transcription Factors Transcription Factors, TFII HDAC1 protein, human Histone Deacetylase 1 Histone Deacetylases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Muscat G E
University of Queensland, Centre for Molecular and Cellular Biology, Ritchie Research Laboratories, B402A, St Lucia 4072, Queensland, Australia. g.guscat@cmcb.uq.edu.au
Burke L J
Downes M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/26.12.2899
Email
g.guscat@cmcb.uq.edu.au
Published
1998-06-15
Pages
2899-907
Language
English
Region
England
NLM ID
0411011
PMCID
PMC147645
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/26.12.2899 PMC Full Text View journal details
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