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  Major satellite repeat RNA stabilize heterochromatin retention of Suv39h enzymes by RNA-nucleosome assocation and RNA:DNA hybrid formation

Camacho, O. V., Galan, C., Swist-Rosowska, K., Ching, R., Gamalinda, M., Karabiber, F., et al. (2017). Major satellite repeat RNA stabilize heterochromatin retention of Suv39h enzymes by RNA-nucleosome assocation and RNA:DNA hybrid formation. eLife, e25293. doi:10.7554/eLife.25293.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-BFCF-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-C2B5-3
Genre: Journal Article

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Valezquez et al..pdf (Publisher version), 9MB
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https://elifesciences.org/articles/25293 (Publisher version)
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 Creators:
Camacho, Oscar Velazquez1, Author
Galan, Carmen1, Author
Swist-Rosowska, Kalina1, Author
Ching, Reagan1, Author
Gamalinda, Michael1, Author
Karabiber, Fethullah2, Author
La Rosa-Velazquez, Inti De1, Author
Engist, Bettina1, Author
Koschorz, Birgit1, Author
Shukeir, Nicholas1, Author
Onishi-Seebacher, Megumi1, Author
van de Nobelen, Suzanne1, Author
Jenuwein, Thomas2, Author              
Affiliations:
1Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, 79108 Freiburg, DE, ou_2243640              
2External Organizations, ou_persistent22              

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 Abstract: The Suv39h1 and Suv39h2 histone lysine methyltransferases are hallmark enzymes at mammalian heterochromatin. We show here that the mouse Suv39h2 enzyme differs from Suv39h1 by containing an N-terminal basic domain that facilitates retention at mitotic chromatin and provides an additional affinity for major satellite repeat RNA. To analyze an RNA-dependent interaction with chromatin, we purified native nucleosomes from mouse ES cells and detect that Suv39h1 and Suv39h2 exclusively associate with poly-nucleosomes. This association was attenuated upon RNaseH incubation and entirely lost upon RNaseA digestion of native chromatin. Major satellite repeat transcripts remain chromatin-associated and have a secondary structure that favors RNA:DNA hybrid formation. Together, these data reveal an RNA-mediated mechanism for the stable chromatin interaction of the Suv39h KMT and suggest a function for major satellite non-coding RNA in the organization of an RNA-nucleosome scaffold as the underlying structure of mouse heterochromatin.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.25293
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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: e25293 Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X