Groucho and dCtBP mediate separate pathways of transcriptional repression in the Drosophila embryo
Open accessAbstract
The precellular Drosophila embryo contains ≈10 well characterized transcriptional repressors. At least half are short-range repressors that must bind within 100 bp of either upstream activators or the core transcription complex to inhibit (or quench) gene expression. The two long-range repressors can function over distances of 1 kilobase or more to silence transcription. Previous studies have shown that three of the five short-range repressors interact with a common corepressor protein, dCtBP. In contrast, the two long-range repressors, Hairy and Dorsal, recruit a different corepressor protein, Groucho. Hairy also was shown to interact with dCtBP, thereby raising the possibility that Groucho and dCtBP are components of a common corepressor complex. To investigate this issue, we have misexpressed wild-type and mutant forms of Hairy in transgenic embryos. Evidence is presented that Hairy-mediated repression depends on the Groucho interaction sequence (WRPW) but not the weak dCtBP motif (PLSLV) present in the native protein. Conversion of the PLSLV motif into an optimal dCtBP interaction sequence (PLDLS) disrupts the activity of an otherwise normal Hairy protein. These results suggest that dCtBP and Groucho mediate separate pathways of transcriptional repression and that the two proteins can inhibit one another when both bind the same repressor.
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Across Bilateria, cell type-specific gene expression in striated muscle cells is controlled by members of the MyoD family of bHLH transcriptional regulators and by regulators of the Mef2 class.
“Across the Bilateria, for example, cell type-specific gene expression in striated muscle cells is controlled by members of the MyoD family of bHLH transcriptional regulators and by regulators of the Mef2 class (Molkentin et al., 1995) (reviewed by Zhang et al., 1999).”
From The last common bilaterian ancestor (2002) · cites this paper as Zhang et al., 1999
The Abstract and Results discuss Hairy, Groucho, and dCtBP in early Drosophila embryos, not regulation of striated-muscle gene expression across Bilateria. Searches for MyoD, Mef2, and muscle-specific regulators found no passage addressing the attributed claim. (LLM, conf=0.77)
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- Authors
- Zhang, H., & Levine, M.
- Affiliations
- University of California, Berkeley (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-01-19
- Volume
- 96
- Issue
- 2
- Pages
- 535-540
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC15171
- OpenAlex
- W2013740909
- Cited by
- 92
- References
- 41
- Citations by year
- 2024: 1 · 2018: 1 · 2016: 1 · 2014: 1 · 2013: 3 · 2012: 2
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM 46638)
- National Institute of General Medical Sciences (R37GM046638, R01GM046638)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- Groucho, transcriptional repression, corepressors, hairy, Drosophila embryo, Dorsal, protein-protein interaction, transcriptional silencing
- MeSH terms
- Alcohol Oxidoreductases, Animals, DNA-Binding Proteins, Drosophila, Nuclear Proteins, Phosphoproteins, Repressor Proteins, Transcription Factors, RNA-Binding Proteins, In Situ Hybridization, Gene Expression Regulation, Developmental, Insect Proteins, Body Patterning, Drosophila Proteins, Animals, Genetically Modified, Embryonic Development, Basic Helix-Loop-Helix Transcription Factors, Basic Helix-Loop-Helix Proteins
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