Oberoi, Jasmeen, Fairall, Louise, Watson, Peter J, Yang, Ji-Chun, Czimmerer, Zsolt, Kampmann, Thorsten, Goult, Benjamin T, Greenwood, Jacquie A, Gooch, John T, Kallenberger, Bettina C, and others. (2011) Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery. Nature structural & molecular biology, 18 (2). pp. 177-184. ISSN 1545-9985. (doi:10.1038/nsmb.1983) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:42119)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: http://dx.doi.org/10.1038/nsmb.1983 |
Abstract
Eukaryotic transcriptional repressors function by recruiting large coregulatory complexes that target histone deacetylase enzymes to gene promoters and enhancers. Transcriptional repression complexes, assembled by the corepressor NCoR and its homolog SMRT, are crucial in many processes, including development and metabolic physiology. The core repression complex involves the recruitment of three proteins, HDAC3, GPS2 and TBL1, to a highly conserved repression domain within SMRT and NCoR. We have used structural and functional approaches to gain insight into the architecture and biological role of this complex. We report the crystal structure of the tetrameric oligomerization domain of TBL1, which interacts with both SMRT and GPS2, and the NMR structure of the interface complex between GPS2 and SMRT. These structures, together with computational docking, mutagenesis and functional assays, reveal the assembly mechanism and stoichiometry of the corepressor complex.
Item Type: | Article |
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DOI/Identification number: | 10.1038/nsmb.1983 |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Ben Goult |
Date Deposited: | 07 Aug 2014 20:13 UTC |
Last Modified: | 05 Nov 2024 10:26 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/42119 (The current URI for this page, for reference purposes) |
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