The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression
Open accessAbstract
Transcriptional repression by Mad-Max heterodimers requires interaction of Mad with the corepressors mSin3A/B. Sin3p, the S. cerevisiae homolog of mSin3, functions in the same pathway as Rpd3p, a protein related to two recently identified mammalian histone deacetylases, HDAC1 and HDAC2. Here, we demonstrate that mSin3A and HDAC1/2 are associated in vivo. HDAC2 binding requires a conserved region of mSin3A capable of mediating transcriptional repression. In addition, Mad1 forms a complex with mSin3 and HDAC2 that contains histone deacetylase activity. Trichostatin A, an inhibitor of histone deacetylases, abolishes Mad repression. We propose that Mad-Max functions by recruiting the mSin3-HDAC corepressor complex that deacetylates nucleosomal histones, producing alterations in chromatin structure that block transcription.
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Cites
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Cited by
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Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription
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Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
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The coregulator exchange in transcriptional functions of nuclear receptors
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Metadata
- Authors
- Laherty, C. D., Yang, W.-M., Sun, J.-M., Davie, J. R., Seto, E., & Eisenman, R. N.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-05
- Volume
- 89
- Issue
- 3
- Pages
- 349-356
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2104788426
- Cited by
- 938
- References
- 48
- FWCI
- 31.27
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Laherty, C. D., Yang, W.-M., Sun, J.-M., Davie, J. R., Seto, E., & Eisenman, R. N. (1997). Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression. Cell. https://doi.org/10.1016/s0092-8674(00)80215-9
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