Arnold Library

Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression.

Laherty, C D and Yang, W M and Sun, J M and Davie, J R and Seto, E and Eisenman, R N (1997) Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell, 89 (3). pp. 349-356. ISSN 0092-8674

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Article URL: http://dx.doi.org/10.1016/S0092-8674(00)80215-9

Abstract

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.

Item Type: Article
Additional Information: This article is freely available at the publisher's website.
DOI: 10.1016/S0092-8674(00)80215-9
PubMed ID: 9150134
Keywords or MeSH Headings: Animals; Cells, Cultured/enzymology; DNA-Binding Proteins/genetics; Gene Expression Regulation, Enzymologic/physiology; Histone Deacetylases/genetics/metabolism; Multienzyme Complexes/genetics/metabolism; Protein Binding/physiology; Protein Structure, Tertiary; Rabbits; Repressor Proteins/chemistry/genetics/metabolism; Saccharomyces cerevisiae Proteins; Transcription Factors/chemistry/genetics/metabolism; Transcription, Genetic/physiology;
Subjects: Molecules > Proteins > Transcription factors
Molecules > Molecular structure
Cellular and Organismal Processes > Genetic processes > Transcription
Depositing User: Library Staff
Date Deposited: 25 Nov 2008 23:00
Last Modified: 07 May 2010 20:38
URI: http://authors.fhcrc.org/id/eprint/164

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