The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3

Guenther, Matthew G.; Barak, Orr; Lazar, Mitchell A.

doi:10.1128/mcb.21.18.6091-6101.2001

Cited by 611Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3

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Guenther, Matthew G., Barak, Orr, Lazar, Mitchell A.·2001·Molecular and Cellular Biology

DOI 10.1128/mcb.21.18.6091-6101.2001PMC PMC87326

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Abstract

Repression of gene transcription is linked to regulation of chromatin structure through deacetylation of core histone amino-terminal tails. This action is mediated by histone deacetylases (HDACs) that function within active multiprotein complexes directed to the promoters of repressed genes. In vivo, HDAC3 forms a stable complex with the SMRT corepressor. The SMRT-HDAC3 complex exhibits histone deacetylase activity, whereas recombinant HDAC3 is an inactive enzyme. Here we report that SMRT functions as an activating cofactor of HDAC3. In contrast, SMRT does not activate the class II HDAC4, with which it also interacts. Activation of HDAC3 is mediated by a deacetylase activating domain (DAD) that includes one of two SANT motifs present in SMRT. A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3. Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity. Using purified components, the SMRT DAD is shown to be necessary and sufficient for activation of HDAC3. Moreover, the DAD is required both for HDAC3 to function enzymatically and for the major repression function of SMRT. Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.

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HDACs 1, 2 and 3 require association with large multisubunit corepressor complexes for maximal activity.
“HDACs 1, 2 and 3 require association with large multisubunit corepressor complexes for maximal activity7-12.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [11]
The Results and Discussion show that HDAC3 needs SMRT or N-CoR for activity, and the Discussion reports that HDAC1 needs components of the NuRD complex. The copy does not establish the same requirement for HDAC2. Moreover, the Abstract says a purified SMRT domain is sufficient to activate HDAC3, so it does not establish that a large multisubunit complex is required for its activity. (LLM, conf=0.88)
Experimental — accuracy not yet measured
The DAD contains an extended SANT-like domain with an amino-terminal DAD-specific motif, and deletion of this motif results in both loss of binding and failure to activate HDAC3.
“The DAD contains an extended SANT-like domain with an amino-terminal DAD-specific motif. Deletion of this motif results in both loss of binding and failure to activate HDAC311.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [11]
The DAD both recruits and activates HDAC3.
“The DAD both recruits and activates HDAC310-12.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [11]

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Authors: Guenther, M. G., Barak, O., & Lazar, M. A.
Affiliations: University of Pennsylvania (US)
ORCID: Guenther, Matthew G.
Lazar, Mitchell A.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2001-09-01
Volume: 21
Issue: 18
Pages: 6091-6101
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.21.18.6091-6101.2001
PMC: PMC87326
OpenAlex: W2118650392
Cited by: 611
References: 71
Citations by year: 2026: 15 · 2025: 14 · 2024: 21 · 2023: 23 · 2022: 22 · 2021: 30 · 2020: 30 · 2019: 25 · 2018: 24 · 2017: 19 · 2016: 25 · 2015: 22 · 2014: 27 · 2013: 32 · 2012: 21
FWCI: 8.96
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: University of Pennsylvania
National Institutes of Health (DK43806)
National Institute of Diabetes and Digestive and Kidney Diseases (DK43806, R01DK045586, DK 45586, R37DK043806, R01DK043806)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: SMRT corepressor, NCoR, HDAC3, HDAC4, transcriptional repression, chromatin deacetylation, histone deacetylase activity
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Chromatin, DNA-Binding Proteins, Enzyme Activation, Gene Expression Regulation, Histone Deacetylases, Molecular Sequence Data, Repressor Proteins, Nuclear Receptor Co-Repressor 2

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The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3

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