SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules
Open accessAbstract
Nucleosome remodeling and deacetylation (NuRD) complexes are co-transcriptional regulators implicated in differentiation, development, and diseases. Methyl-CpG binding domain (MBD) proteins play an essential role in recruitment of NuRD complexes to their target sites in chromatin. The related SHREC complex in fission yeast drives transcriptional gene silencing in heterochromatin through cooperation with HP1 proteins. How remodeler and histone deacetylase (HDAC) cooperate within NuRD complexes remains unresolved. We determined that in SHREC the two modules occupy distant sites on the scaffold protein Clr1 and that repressive activity of SHREC can be modulated by the expression level of the HDAC-associated Clr1 domain alone. Moreover, the crystal structure of Clr2 reveals an MBD-like domain mediating recruitment of the HDAC module to heterochromatin. Thus, SHREC bi-functionality is organized in two separate modules with separate recruitment mechanisms, which work together to elicit transcriptional silencing at heterochromatic loci.
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HDAC10 PDAC-ΨDAC heterodomain assembly resembles HDAC6 heterodomain assembly and HDAC homodomain assembly in Schizosaccharomyces pombe Clr3.
“HDAC10 PDAC-ΨDAC heterodomain assembly resembles HDAC6 heterodomain assembly and HDAC homodomain assembly in Schizosaccharomyces pombe Clr3 (Supplementary Fig. 5)2728.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [28]
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- Authors
- Job, G., Brugger, C., Xu, T., Lowe, B. R., Pfister, Y., Qu, C., Shanker, S., Baños Sanz, J. I., Partridge, J. F., & Schalch, T.
- Affiliations
- St. Jude Children's Research Hospital (US)
- University of Geneva (CH)
- Corresponding author
- Partridge, Janet F.
- Schalch, Thomas
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2016-04
- Volume
- 62
- Issue
- 2
- Pages
- 207-221
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC4890606
- OpenAlex
- W2337251005
- Cited by
- 55
- References
- 44
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 13 · 2023: 5 · 2022: 6 · 2021: 7 · 2020: 4 · 2019: 4 · 2018: 4 · 2017: 6 · 2016: 1 · 2014: 1
- FWCI
- 2.60
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 385 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Archive ouverte UNIGE (University of Geneva) (acceptedVersion, other-oa)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Institutes of Health (CCSG 2 P30 CA21765, GM084045)
- American Lebanese Syrian Associated Charities
- Cold Spring Harbor Laboratory
- Société Académique de Genève
- Fondation Ernst et Lucie Schmidheiny
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- heterochromatin, transcriptional silencing, NuRD complex, methyl-CpG binding domain, histone deacetylase, nucleosome remodeling, HP1 proteins, Schizosaccharomyces pombe, chromatin remodeling, protein crystal structure
- MeSH terms
- Acetylation, Binding Sites, DNA, Fungal, Heterochromatin, Models, Molecular, Nucleosomes, Protein Binding, Protein Conformation, Protein Processing, Post-Translational, RNA, Fungal, Schizosaccharomyces, Structure-Activity Relationship, Transcription Factors, Transcription, Genetic, Gene Expression Regulation, Fungal, CpG Islands, Gene Silencing, Schizosaccharomyces pombe Proteins, Chromatin Assembly and Disassembly, Protein Interaction Domains and Motifs, Mi-2 Nucleosome Remodeling and Deacetylase Complex
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