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  Prdm3 and Prdm16 are H3K9me1 Methyltransferases Required for Mammalian Heterochromatin Integrity

Pinheiro, I., Margueron, R., Shukeir, N., Eisold, M., Fritzsch, C., Richter, F. M., et al. (2012). Prdm3 and Prdm16 are H3K9me1 Methyltransferases Required for Mammalian Heterochromatin Integrity. Cell, 150, 948-960.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-8CDA-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-8CDE-3
Genre: Journal Article

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 Creators:
Pinheiro, Ines1, Author
Margueron, Raphael, Author
Shukeir, Nicholas1, Author
Eisold, Michael2, Author              
Fritzsch, Christoph1, Author
Richter, Florian M.1, Author
Mittler, Gerhard3, Author              
Genoud, Christel, Author
Goyama, Susumu, Author
Kurokawa, Mineo, Author
Son, Jinsook, Author
Reinberg, Danny, Author
Lachner, Monika1, Author
Jenuwein, Thomas2, Author              
Affiliations:
1Max Planck Society, ou_persistent13              
2Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243644              
3Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243641              

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 Abstract: Heterochromatin serves important functions, protecting genome integrity and stabilizing gene expression programs. Although the Suv39h methyltransferases (KMTs) are known to ensure pericentric H3K9me3 methylation, the mechanisms that initiate and maintain mammalian heterochromatin organization remain elusive. We developed a biochemical assay and used in vivo analyses in mouse embryonic fibroblasts to identify Prdm3 and Prdm16 as redundant H3K9me1-specific KMTs that direct cytoplasmic H3K9me1 methylation. The H3K9me1 is converted in the nucleus to H3K9me3 by the Suv39h enzymes to reinforce heterochromatin. Simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Most strikingly, DNA-FISH and electron microscopy reveal that combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina. Our data identify Prdm3 and Prdm16 as H3K9me1 methyltransferases and expose a functional framework in which anchoring to the nuclear periphery helps maintain the integrity of mammalian heterochromatin.

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Language(s): eng - English
 Dates: 2012-08-31
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 634417
 Degree: -

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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 150 Sequence Number: - Start / End Page: 948 - 960 Identifier: -