ArticleMolecular & general genetics : MGG1994
The yeast SIN3 gene product negatively regulates the activity of the human progesterone receptor and positively regulates the activities of GAL4 and the HAP1 activator.
Article in Molecular & general genetics : MGG, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 39 citations in OpenAlex.
- A long journey to the discovery of nuclear receptor coactivator existence, physiology, pathology, and therapy.The Journal of biological chemistry · 2025Article
- SAP30 promotes breast tumor progression by bridging the transcriptional corepressor SIN3 complex and MLL1.The Journal of clinical investigation · 2023Article
- Promoter recruitment of corepressors Sin3 and Cyc8 by activator proteins of the yeast Saccharomyces cerevisiae.Current genetics · 2017Article
- Genome-wide studies reveal novel and distinct biological pathways regulated by SIN3 isoforms.BMC genomics · 2016Article
- Article
- Correlation between MMP-13 and HDAC7 expression in human knee osteoarthritis.Modern rheumatology · 2010Article
- The highly conserved region of the co-repressor Sin3A functionally interacts with the co-repressor Alien.Nucleic acids research · 2004Article
- Chromatin acetylation and remodeling at the Cis promoter during STAT5-induced transcription.Nucleic acids research · 2003Article
- Deacetylase activity is required for recruitment of the basal transcription machinery and transactivation by STAT5.Molecular and cellular biology · 2003Article
- Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- The yeast Ada complex mediates the ligand-dependent activation function AF-2 of retinoid X and estrogen receptors.Genes & development · 1998Article
- Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- A nuclear hormone receptor-associated protein that inhibits transactivation by the thyroid hormone and retinoic acid receptors.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Genetic interactions between SIN3 mutations and the Saccharomyces cerevisiae transcriptional activators encoded by MCM1, STE12, and SWI1.Molecular & general genetics : MGG · 1994Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The activation of gene transcription in eukaryotic organisms is regulated by sequence-specific DNA-binding proteins as well as by non-DNA-binding proteins. In this report we describe the modulatory functions of a non-DNA-binding protein, SIN3 (also known as SDI1, UME4, RPD1, and GAM2) on the transactivation properties of the human progesterone receptor (hPR), GAL4, and the HAP1 activator in yeast. Our data suggest that SIN3 is a dual function protein. It negatively regulates the transcriptional activities of hPR-A and hPR-B by affecting the N-terminal activation domain (AF1). SIN3 positively regulates the transcriptional activities of GAL4 and the HAP1 activator. However, it has no effect on the transcriptional activities of the human glucocorticoid receptor (hGR) and GCN4. The SIN3 protein contains four copies of a paired amphipathic helix (PAH) motif. Deletion analysis of the SIN3 PAH motifs shows that the PAH3 motif is essential for SIN3-mediated regulation of hPR, GAL4, and the HAP1 activator. In contrast, the PAH1, PAH2, and PAH4 motifs are not required for SIN3-mediated regulation of these activators. Additionally, we examined the mechanism(s) by which the SIN3 protein modulate the activities of various activators. We are unable to demonstrate the direct interaction of SIN3 protein with these activators using the yeast two-hybrid system or co-immunoprecipitation. These data suggest that SIN3 regulates the transactivation functions of hPR, GAL4, and the HAP1 activator by an indirect mechanism.
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