Author:
Zamir I,Zhang J,Lazar M A
Abstract
We have defined two principles of corepressor function that account for differences in transcriptional repression by nuclear hormone receptors (NHRs). First, we have determined that receptor stoichiometry is a crucial determinant of transcriptional repression mediated by the corepressors N-CoR and SMRT. This provides a molecular explanation for the observation that NHRs repress transcription as dimers but not monomers. Second, corepressor function is restricted by steric effects related to DNA binding in a receptor-specific manner. Thus, although N-CoR and SMRT are capable of binding to several NHRs in solution, they are highly selective about receptor binding on DNA, a context that reflects their in vivo function more accurately. These stoichiometric and steric principles govern specific interactions between corepressors and NHRs, thus providing evidence that N-CoR and SMRT do not serve redundant functions but rather contribute to receptor-specific transcriptional repression.
Publisher
Cold Spring Harbor Laboratory
Subject
Developmental Biology,Genetics
Reference62 articles.
1. A functional Rev-erb alpha responsive element located in the human Rev-erb alpha promoter mediates a repressing activity.
2. Ausubel, F.M., R. Brent, R. Kingston, D.D. Moore, J.A. Smith, J.G. Seidman, and K. Struhl. 1987. Current protocols in molecular biology. Wiley Interscience/Greene Publishing, New York, NY.
3. A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor.;EMBO J.,1992
4. The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing.;Mol. Cell. Biol.,1995
5. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor.;EMBO J.,1994
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