Cited by 606Genomics and Chromatin DynamicsEpigenetics and DNA MethylationNuclear Structure and Function

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Step-Wise Methylation of Histone H3K9 Positions Heterochromatin at the Nuclear Periphery

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Towbin, Benjamin D., González-Aguilera, Cristina, Sack, Ragna, Gaidatzis, Dimos, Kalck, Véronique, Meister, Peter, Askjaer, Peter, Gasser, Susan M.·2012·Cell

DOI 10.1016/j.cell.2012.06.051

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Abstract

The factors that sequester transcriptionally repressed heterochromatin at the nuclear periphery are currently unknown. In a genome-wide RNAi screen, we found that depletion of S-adenosylmethionine (SAM) synthetase reduces histone methylation globally and causes derepression and release of heterochromatin from the nuclear periphery in Caenorhabditis elegans embryos. Analysis of histone methyltransferases (HMTs) showed that elimination of two HMTs, MET-2 and SET-25, mimics the loss of SAM synthetase, abrogating the perinuclear attachment of heterochromatic transgenes and of native chromosomal arms rich in histone H3 lysine 9 methylation. The two HMTs target H3K9 in a consecutive fashion: MET-2, a SETDB1 homolog, mediates mono- and dimethylation, and SET-25, a previously uncharacterized HMT, deposits H3K9me3. SET-25 colocalizes with its own product in perinuclear foci, in a manner dependent on H3K9me3, but not on its catalytic domain. This colocalization suggests an autonomous, self-reinforcing mechanism for the establishment and propagation of repeat-rich heterochromatin.

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Authors: Towbin, B. D., González-Aguilera, C., Sack, R., Gaidatzis, D., Kalck, V., Meister, P., Askjaer, P., & Gasser, S. M.
Affiliations: University of Basel (CH)
Friedrich Miescher Institute (CH)
Consejo Superior de Investigaciones Científicas (ES)
Corresponding author: Gasser, Susan M.
ORCID: Towbin, Benjamin D.
Sack, Ragna
Gaidatzis, Dimos
Meister, Peter
Askjaer, Peter
Gasser, Susan M.
Venue: Cell
Publisher: Elsevier BV
Published: 2012-08
Volume: 150
Issue: 5
Pages: 934-947
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2012.06.051
OpenAlex: W2033160626
Cited by: 597
References: 54
Citations by year: 2026: 29 · 2025: 33 · 2024: 39 · 2023: 24 · 2022: 36 · 2021: 42 · 2020: 51 · 2019: 42 · 2018: 57 · 2017: 45 · 2016: 56 · 2015: 48 · 2014: 42 · 2013: 45 · 2012: 7
FWCI: 18.22
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, 428 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
BORIS (University Library Bern) (submittedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, other-oa)
Topics: 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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: heterochromatin, nuclear periphery, histone H3 lysine 9 methylation, histone methyltransferase, MET-2, S-adenosylmethionine synthetase, H3K9me3, chromatin condensation, Caenorhabditis elegans embryo, RNAi screen
MeSH terms: Animals, Cell Nucleus, Chromosomes, Embryo, Nonmammalian, Heterochromatin, Histones, Methionine Adenosyltransferase, Methylation, Mutation, Histone-Lysine N-Methyltransferase, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Lamins, Genome, Helminth

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Step-Wise Methylation of Histone H3K9 Positions Heterochromatin at the Nuclear Periphery

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